메뉴 건너뛰기




Volumn 5, Issue , 2012, Pages 139-163

Structure and folding of outer membrane proteins

Author keywords

barrel proteins; Cylindrical barrels; Membrane protein folding; Membrane protein structure; Multidomain structures; OMPs

Indexed keywords


EID: 84882744404     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00514-2     Document Type: Chapter
Times cited : (10)

References (192)
  • 1
    • 0026331041 scopus 로고
    • Molecular architecture and electrostatic properties of a bacterial porin
    • Weiss M.S., Abele U., Weckesser J., Welte W., Schiltz E., Schulz G.E. Molecular architecture and electrostatic properties of a bacterial porin. Science 1991, 254:1627-1630.
    • (1991) Science , vol.254 , pp. 1627-1630
    • Weiss, M.S.1    Abele, U.2    Weckesser, J.3    Welte, W.4    Schiltz, E.5    Schulz, G.E.6
  • 2
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • White S.H., Wimley W.C. Membrane protein folding and stability: Physical principles. Annu. Rev. Biophys. Biomol. Struct. 1999, 28:319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 3
    • 36749026606 scopus 로고    scopus 로고
    • The process of folding proteins into membranes: Progress and challenges
    • Stanley A.M., Fleming K.G. The process of folding proteins into membranes: Progress and challenges. Arch. Biochem. Biophys. 2008, 469:46-66.
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 46-66
    • Stanley, A.M.1    Fleming, K.G.2
  • 4
    • 0030220261 scopus 로고    scopus 로고
    • Porins: General to specific, native to engineered passive pores
    • Schulz G.E. Porins: General to specific, native to engineered passive pores. Curr. Opin. Struct. Biol. 1996, 6:485-490.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 485-490
    • Schulz, G.E.1
  • 6
    • 77449153905 scopus 로고    scopus 로고
    • Cation-selective pathway of OmpF porin revealed by anomalous X-ray diffraction
    • Dhakshnamoorthy B., Raychaudhury S., Blachowicz L., Roux B. Cation-selective pathway of OmpF porin revealed by anomalous X-ray diffraction. J. Mol. Biol. 2009, 396:293-300.
    • (2009) J. Mol. Biol. , vol.396 , pp. 293-300
    • Dhakshnamoorthy, B.1    Raychaudhury, S.2    Blachowicz, L.3    Roux, B.4
  • 7
    • 77951057326 scopus 로고    scopus 로고
    • Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB
    • Tanabe M., Nimigean C.M., Iverson T.M. Structural basis for solute transport, nucleotide regulation, and immunological recognition of Neisseria meningitidis PorB. Proc. Natl. Acad. Sci. USA 2010, 107:6811-6816.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 6811-6816
    • Tanabe, M.1    Nimigean, C.M.2    Iverson, T.M.3
  • 8
    • 0029644059 scopus 로고    scopus 로고
    • Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway
    • Dutzler R., Wang Y.F., Rizkallah P., Rosenbusch J.P., Schirmer T. Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 1996, 4:127-134.
    • (1996) Structure , vol.4 , pp. 127-134
    • Dutzler, R.1    Wang, Y.F.2    Rizkallah, P.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 9
    • 0031565721 scopus 로고    scopus 로고
    • Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin
    • Wang Y.F., Dutzler R., Rizkallah P.J., Rosenbusch J.P., Schirmer T. Channel specificity: Structural basis for sugar discrimination and differential flux rates in maltoporin. J. Mol. Biol. 1997, 272:56-63.
    • (1997) J. Mol. Biol. , vol.272 , pp. 56-63
    • Wang, Y.F.1    Dutzler, R.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 10
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • Forst D., Welte W., Wacker T., Diederichs K. Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 1998, 5:37-46.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 11
    • 0017671931 scopus 로고
    • Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants
    • Chai T.J., Foulds J. Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants. Biochim. Biophys. Acta 1977, 493:210-215.
    • (1977) Biochim. Biophys. Acta , vol.493 , pp. 210-215
    • Chai, T.J.1    Foulds, J.2
  • 12
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • Grizot S., Buchanan S.K. Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol. Microbiol. 2004, 51:1027-1037.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 13
    • 0028263998 scopus 로고
    • The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan
    • De Mot R., Vanderleyden J. The C-terminal sequence conservation between OmpA-related outer membrane proteins and MotB suggests a common function in both gram-positive and gram-negative bacteria, possibly in the interaction of these domains with peptidoglycan. Mol. Microbiol. 1994, 12:333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • De Mot, R.1    Vanderleyden, J.2
  • 14
    • 0029092472 scopus 로고
    • Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins
    • Koebnik R. Proposal for a peptidoglycan-associating alpha-helical motif in the C-terminal regions of some bacterial cell-surface proteins. Mol. Microbiol. 1995, 16:1269-1270.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1269-1270
    • Koebnik, R.1
  • 15
    • 0036070655 scopus 로고    scopus 로고
    • Identification of Escherichia coli outer membrane protein A receptor on human brain microvascular endothelial cells
    • Prasadarao N.V. Identification of Escherichia coli outer membrane protein A receptor on human brain microvascular endothelial cells. Infect. Immun. 2002, 70:4556-4563.
    • (2002) Infect. Immun. , vol.70 , pp. 4556-4563
    • Prasadarao, N.V.1
  • 16
    • 30944444979 scopus 로고    scopus 로고
    • Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility
    • Barrios A.F., Zuo R., Ren D., Wood T.K. Hha, YbaJ, and OmpA regulate Escherichia coli K12 biofilm formation and conjugation plasmids abolish motility. Biotechnol. Bioeng. 2006, 93:188-200.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 188-200
    • Barrios, A.F.1    Zuo, R.2    Ren, D.3    Wood, T.K.4
  • 17
    • 0033570111 scopus 로고    scopus 로고
    • The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence
    • Vogt J., Schulz G.E. The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence. Structure 1999, 7:1301-1309.
    • (1999) Structure , vol.7 , pp. 1301-1309
    • Vogt, J.1    Schulz, G.E.2
  • 18
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A., Schulz G.E. Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 1998, 5:1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 19
    • 0026785288 scopus 로고
    • Pore-forming activity of OmpA protein of Escherichia coli
    • Sugawara E., Nikaido H. Pore-forming activity of OmpA protein of Escherichia coli. J. Biol. Chem. 1992, 267:2507-2511.
    • (1992) J. Biol. Chem. , vol.267 , pp. 2507-2511
    • Sugawara, E.1    Nikaido, H.2
  • 20
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
    • Arora A., Abildgaard F., Bushweller J.H., Tamm L.K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 2001, 8:334-338.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 21
    • 24944512361 scopus 로고    scopus 로고
    • Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae
    • Nandi B., Nandy R.K., Sarkar A., Ghose A.C. Structural features, properties and regulation of the outer-membrane protein W (OmpW) of Vibrio cholerae. Microbiology 2005, 151:2975-2986.
    • (2005) Microbiology , vol.151 , pp. 2975-2986
    • Nandi, B.1    Nandy, R.K.2    Sarkar, A.3    Ghose, A.C.4
  • 22
    • 33645779427 scopus 로고    scopus 로고
    • The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel
    • Hong H., Patel D.R., Tamm L.K., van den Berg B. The outer membrane protein OmpW forms an eight-stranded beta-barrel with a hydrophobic channel. J. Biol. Chem. 2006, 281:7568-7577.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7568-7577
    • Hong, H.1    Patel, D.R.2    Tamm, L.K.3    van den Berg, B.4
  • 23
    • 58549093720 scopus 로고    scopus 로고
    • Crystal structure of a major outer membrane protein from Thermus thermophilus HB27
    • Brosig A., Nesper J., Boos W., Welte W., Diederichs K. Crystal structure of a major outer membrane protein from Thermus thermophilus HB27. J. Mol. Biol. 2009, 385:1445-1455.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1445-1455
    • Brosig, A.1    Nesper, J.2    Boos, W.3    Welte, W.4    Diederichs, K.5
  • 25
    • 0032933020 scopus 로고    scopus 로고
    • Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo
    • Dekker N., Tommassen J., Verheij H.M. Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo. J. Bacteriol. 1999, 181:3281-3283.
    • (1999) J. Bacteriol. , vol.181 , pp. 3281-3283
    • Dekker, N.1    Tommassen, J.2    Verheij, H.M.3
  • 29
    • 0035903650 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site
    • Vandeputte-Rutten L., Kramer R.A., Kroon J., Dekker N., Egmond M.R., Gros P. Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site. EMBO J. 2001, 20:5033-5039.
    • (2001) EMBO J. , vol.20 , pp. 5033-5039
    • Vandeputte-Rutten, L.1    Kramer, R.A.2    Kroon, J.3    Dekker, N.4    Egmond, M.R.5    Gros, P.6
  • 31
    • 13244259151 scopus 로고    scopus 로고
    • Folding and particle assembly are disrupted by single-point mutations near the autocatalytic cleavage site of Nudaurelia capensis omega virus capsid protein
    • Taylor D.J., Johnson J.E. Folding and particle assembly are disrupted by single-point mutations near the autocatalytic cleavage site of Nudaurelia capensis omega virus capsid protein. Protein Sci. 2005, 14:401-408.
    • (2005) Protein Sci. , vol.14 , pp. 401-408
    • Taylor, D.J.1    Johnson, J.E.2
  • 32
    • 4444258925 scopus 로고    scopus 로고
    • Crystal structure of the bacterial nucleoside transporter Tsx
    • Ye J., van den Berg B. Crystal structure of the bacterial nucleoside transporter Tsx. EMBO J. 2004, 23:3187-3195.
    • (2004) EMBO J. , vol.23 , pp. 3187-3195
    • Ye, J.1    van den Berg, B.2
  • 33
    • 2642522855 scopus 로고    scopus 로고
    • Crystal structure of the long-chain fatty acid transporter FadL
    • van den Berg B., Black P.N., Clemons W.M., Rapoport T.A. Crystal structure of the long-chain fatty acid transporter FadL. Science 2004, 304:1506-1509.
    • (2004) Science , vol.304 , pp. 1506-1509
    • van den Berg, B.1    Black, P.N.2    Clemons, W.M.3    Rapoport, T.A.4
  • 34
    • 62649094413 scopus 로고    scopus 로고
    • Transmembrane passage of hydrophobic compounds through a protein channel wall
    • Hearn E.M., Patel D.R., Lepore B.W., Indic M., van den Berg B. Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 2009, 458:367-370.
    • (2009) Nature , vol.458 , pp. 367-370
    • Hearn, E.M.1    Patel, D.R.2    Lepore, B.W.3    Indic, M.4    van den Berg, B.5
  • 36
    • 46149094595 scopus 로고    scopus 로고
    • New substrates for TonB-dependent transport: Do we only see the 'tip of the iceberg'?
    • Schauer K., Rodionov D.A., de Reuse H. New substrates for TonB-dependent transport: Do we only see the 'tip of the iceberg'?. Trends Biochem. Sci. 2008, 33:330-338.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 330-338
    • Schauer, K.1    Rodionov, D.A.2    de Reuse, H.3
  • 37
    • 34347369410 scopus 로고    scopus 로고
    • TonB system, in vivo assays and characterization
    • Postle K. TonB system, in vivo assays and characterization. Methods Enzymol. 2007, 422:245-269.
    • (2007) Methods Enzymol. , vol.422 , pp. 245-269
    • Postle, K.1
  • 39
    • 0042508859 scopus 로고    scopus 로고
    • Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
    • Yue W.W., Grizot S., Buchanan S.K. Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J. Mol. Biol. 2003, 332:353-368.
    • (2003) J. Mol. Biol. , vol.332 , pp. 353-368
    • Yue, W.W.1    Grizot, S.2    Buchanan, S.K.3
  • 41
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: Structure of the BtuB:TonB complex
    • Shultis D.D., Purdy M.D., Banchs C.N., Wiener M.C. Outer membrane active transport: Structure of the BtuB:TonB complex. Science 2006, 312:1396-1399.
    • (2006) Science , vol.312 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 42
    • 34447339675 scopus 로고    scopus 로고
    • Mechanics of force propagation in TonB-dependent outer membrane transport
    • Gumbart J., Wiener M.C., Tajkhorshid E. Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys. J. 2007, 93:496-504.
    • (2007) Biophys. J. , vol.93 , pp. 496-504
    • Gumbart, J.1    Wiener, M.C.2    Tajkhorshid, E.3
  • 43
    • 0033937939 scopus 로고    scopus 로고
    • Multiple pathways allow protein secretion across the bacterial outer membrane
    • Thanassi D.G., Hultgren S.J. Multiple pathways allow protein secretion across the bacterial outer membrane. Curr. Opin. Cell Biol. 2000, 12:420-430.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 420-430
    • Thanassi, D.G.1    Hultgren, S.J.2
  • 44
    • 48649107476 scopus 로고    scopus 로고
    • The type VI secretion toolkit
    • Cascales E. The type VI secretion toolkit. EMBO Rep. 2008, 9:735-741.
    • (2008) EMBO Rep. , vol.9 , pp. 735-741
    • Cascales, E.1
  • 45
    • 35848952765 scopus 로고    scopus 로고
    • Protein secretion in gram-negative bacteria via the autotransporter pathway
    • Dautin N., Bernstein H.D. Protein secretion in gram-negative bacteria via the autotransporter pathway. Annu. Rev. Microbiol. 2007, 61:89-112.
    • (2007) Annu. Rev. Microbiol. , vol.61 , pp. 89-112
    • Dautin, N.1    Bernstein, H.D.2
  • 46
    • 34548064837 scopus 로고    scopus 로고
    • Structure and function of the bacterial Sec translocon
    • Gold V.A., Duong F., Collinson I. Structure and function of the bacterial Sec translocon. Mol. Membr. Biol. 2007, 24:387-394.
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 387-394
    • Gold, V.A.1    Duong, F.2    Collinson, I.3
  • 48
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng G., Surana N.K., Geme J.W., Waksman G. Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. EMBO J. 2006, 25:2297-2304.
    • (2006) EMBO J. , vol.25 , pp. 2297-2304
    • Meng, G.1    Surana, N.K.2    Geme, J.W.3    Waksman, G.4
  • 50
    • 33747790227 scopus 로고    scopus 로고
    • The turn of the screw: Variations of the abundant beta-solenoid motif in passenger domains of type V secretory proteins
    • Kajava A.V., Steven A.C. The turn of the screw: Variations of the abundant beta-solenoid motif in passenger domains of type V secretory proteins. J. Struct. Biol. 2006, 155:306-315.
    • (2006) J. Struct. Biol. , vol.155 , pp. 306-315
    • Kajava, A.V.1    Steven, A.C.2
  • 51
    • 0033940002 scopus 로고    scopus 로고
    • Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli
    • Zgurskaya H.I., Nikaido H. Cross-linked complex between oligomeric periplasmic lipoprotein AcrA and the inner-membrane-associated multidrug efflux pump AcrB from Escherichia coli. J. Bacteriol. 2000, 182:4264-4267.
    • (2000) J. Bacteriol. , vol.182 , pp. 4264-4267
    • Zgurskaya, H.I.1    Nikaido, H.2
  • 52
    • 0035091452 scopus 로고    scopus 로고
    • Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element
    • Kobayashi K., Tsukagoshi N., Aono R. Suppression of hypersensitivity of Escherichia coli acrB mutant to organic solvents by integrational activation of the acrEF operon with the IS1 or IS2 element. J. Bacteriol. 2001, 183:2646-2653.
    • (2001) J. Bacteriol. , vol.183 , pp. 2646-2653
    • Kobayashi, K.1    Tsukagoshi, N.2    Aono, R.3
  • 53
    • 0034702177 scopus 로고    scopus 로고
    • Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
    • Koronakis V., Sharff A., Koronakis E., Luisi B., Hughes C. Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export. Nature 2000, 405:914-919.
    • (2000) Nature , vol.405 , pp. 914-919
    • Koronakis, V.1    Sharff, A.2    Koronakis, E.3    Luisi, B.4    Hughes, C.5
  • 57
    • 66149150292 scopus 로고    scopus 로고
    • Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC
    • Huang Y., Smith B.S., Chen L.X., Baxter R.H., Deisenhofer J. Insights into pilus assembly and secretion from the structure and functional characterization of usher PapC. Proc. Natl. Acad. Sci. USA 2009, 106:7403-7407.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7403-7407
    • Huang, Y.1    Smith, B.S.2    Chen, L.X.3    Baxter, R.H.4    Deisenhofer, J.5
  • 58
  • 60
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • Hiller S., Garces R.G., Malia T.J., Orekhov V.Y., Colombini M., Wagner G. Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 2008, 321:1206-1210.
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 63
    • 34249696578 scopus 로고    scopus 로고
    • The supramolecular assemblies of voltage-dependent anion channels in the native membrane
    • Hoogenboom B.W., Suda K., Engel A., Fotiadis D. The supramolecular assemblies of voltage-dependent anion channels in the native membrane. J. Mol. Biol. 2007, 370:246-255.
    • (2007) J. Mol. Biol. , vol.370 , pp. 246-255
    • Hoogenboom, B.W.1    Suda, K.2    Engel, A.3    Fotiadis, D.4
  • 64
    • 14244269224 scopus 로고    scopus 로고
    • Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria
    • Zalk R., Israelson A., Garty E.S., Azoulay-Zohar H., Shoshan-Barmatz V. Oligomeric states of the voltage-dependent anion channel and cytochrome c release from mitochondria. Biochem. J. 2005, 386:73-83.
    • (2005) Biochem. J. , vol.386 , pp. 73-83
    • Zalk, R.1    Israelson, A.2    Garty, E.S.3    Azoulay-Zohar, H.4    Shoshan-Barmatz, V.5
  • 65
    • 0027222842 scopus 로고
    • Physical organization of lipids in the cell wall of Mycobacterium chelonae
    • Nikaido H., Kim S.H., Rosenberg E.Y. Physical organization of lipids in the cell wall of Mycobacterium chelonae. Mol. Microbiol. 1993, 8:1025-1030.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1025-1030
    • Nikaido, H.1    Kim, S.H.2    Rosenberg, E.Y.3
  • 66
    • 0026655895 scopus 로고
    • Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols
    • Paul T.R., Beveridge T.J. Reevaluation of envelope profiles and cytoplasmic ultrastructure of mycobacteria processed by conventional embedding and freeze-substitution protocols. J. Bacteriol. 1992, 174:6508-6517.
    • (1992) J. Bacteriol. , vol.174 , pp. 6508-6517
    • Paul, T.R.1    Beveridge, T.J.2
  • 67
    • 1242352009 scopus 로고    scopus 로고
    • The structure of a mycobacterial outer-membrane channel
    • Faller M., Niederweis M., Schulz G.E. The structure of a mycobacterial outer-membrane channel. Science 2004, 303:1189-1192.
    • (2004) Science , vol.303 , pp. 1189-1192
    • Faller, M.1    Niederweis, M.2    Schulz, G.E.3
  • 68
    • 0036096326 scopus 로고    scopus 로고
    • Cellular impermeability and uptake of biocides and antibiotics in gram-positive bacteria and mycobacteria
    • Lambert P.A. Cellular impermeability and uptake of biocides and antibiotics in gram-positive bacteria and mycobacteria. J. Appl. Microbiol. 2002, 92(Suppl):46S-54S.
    • (2002) J. Appl. Microbiol. , vol.92 , Issue.SUPPL
    • Lambert, P.A.1
  • 69
    • 43449090997 scopus 로고    scopus 로고
    • A putative alpha-helical porin from Corynebacterium glutamicum
    • Ziegler K., Benz R., Schulz G.E. A putative alpha-helical porin from Corynebacterium glutamicum. J. Mol. Biol. 2008, 379:482-491.
    • (2008) J. Mol. Biol. , vol.379 , pp. 482-491
    • Ziegler, K.1    Benz, R.2    Schulz, G.E.3
  • 71
  • 72
    • 0025297583 scopus 로고
    • The signal peptide
    • von Heijne G. The signal peptide. J. Membr. Biol. 1990, 115:195-201.
    • (1990) J. Membr. Biol. , vol.115 , pp. 195-201
    • von Heijne, G.1
  • 73
    • 28544442609 scopus 로고    scopus 로고
    • Protein translocation across biological membranes
    • Wickner W., Schekman R. Protein translocation across biological membranes. Science 2005, 310:1452-1456.
    • (2005) Science , vol.310 , pp. 1452-1456
    • Wickner, W.1    Schekman, R.2
  • 74
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
    • Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J. Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Proc. Natl. Acad. Sci. USA 2007, 104:6400-6405.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 6400-6405
    • Sklar, J.G.1    Wu, T.2    Gronenberg, L.S.3    Malinverni, J.C.4    Kahne, D.5    Silhavy, T.J.6
  • 75
    • 1842471109 scopus 로고    scopus 로고
    • Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
    • Voulhoux R., Tommassen J. Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly. Res. Microbiol. 2004, 155:129-135.
    • (2004) Res. Microbiol. , vol.155 , pp. 129-135
    • Voulhoux, R.1    Tommassen, J.2
  • 76
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D. Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 2005, 121:235-245.
    • (2005) Cell , vol.121 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 77
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan C.L., Kim S., Kahne D. Reconstitution of outer membrane protein assembly from purified components. Science 2010, 328:890-892.
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 78
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim S., Malinverni J.C., Sliz P., Silhavy T.J., Harrison S.C., Kahne D. Structure and function of an essential component of the outer membrane protein assembly machine. Science 2007, 317:961-964.
    • (2007) Science , vol.317 , pp. 961-964
    • Kim, S.1    Malinverni, J.C.2    Sliz, P.3    Silhavy, T.J.4    Harrison, S.C.5    Kahne, D.6
  • 81
    • 0030010702 scopus 로고    scopus 로고
    • In vivo membrane assembly of split variants of the E. coli outer membrane protein OmpA
    • Koebnik R. In vivo membrane assembly of split variants of the E. coli outer membrane protein OmpA. EMBO J. 1996, 15:3529-3537.
    • (1996) EMBO J. , vol.15 , pp. 3529-3537
    • Koebnik, R.1
  • 82
    • 0029128758 scopus 로고
    • Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA
    • Koebnik R., Kramer L. Membrane assembly of circularly permuted variants of the E. coli outer membrane protein OmpA. J. Mol. Biol. 1995, 250:617-626.
    • (1995) J. Mol. Biol. , vol.250 , pp. 617-626
    • Koebnik, R.1    Kramer, L.2
  • 83
    • 0001095437 scopus 로고
    • Studies on the gross structure, cross-linkages, and terminal sequences in ribonuclease
    • Anfinsen C.B., Redfield R.R., Choate W.L., Page J., Carroll W.R. Studies on the gross structure, cross-linkages, and terminal sequences in ribonuclease. J. Biol. Chem. 1954, 207:201-210.
    • (1954) J. Biol. Chem. , vol.207 , pp. 201-210
    • Anfinsen, C.B.1    Redfield, R.R.2    Choate, W.L.3    Page, J.4    Carroll, W.R.5
  • 84
    • 0345861754 scopus 로고    scopus 로고
    • The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
    • Gentle I., Gabriel K., Beech P., Waller R., Lithgow T. The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria. J. Cell Biol. 2004, 164:19-24.
    • (2004) J. Cell Biol. , vol.164 , pp. 19-24
    • Gentle, I.1    Gabriel, K.2    Beech, P.3    Waller, R.4    Lithgow, T.5
  • 86
    • 0025081330 scopus 로고
    • Refolding of an integral membrane protein: OmpA of Escherichia coli
    • Dornmair K., Kiefer H., Jähnig F. Refolding of an integral membrane protein: OmpA of Escherichia coli. J. Biol. Chem. 1990, 265:18907-18911.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18907-18911
    • Dornmair, K.1    Kiefer, H.2    Jähnig, F.3
  • 87
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • Hong H., Tamm L.K. Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl. Acad. Sci. USA 2004, 101:4065-4070.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 88
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • Tamm L.K., Hong H., Liang B. Folding and assembly of beta-barrel membrane proteins. Biochim. Biophys. Acta 2004, 1666:250-263.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 89
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • Kleinschmidt J.H., Tamm L.K. Secondary and tertiary structure formation of the beta-barrel membrane protein OmpA is synchronized and depends on membrane thickness. J. Mol. Biol. 2002, 324:319-330.
    • (2002) J. Mol. Biol. , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 90
    • 0032832765 scopus 로고    scopus 로고
    • Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
    • Kleinschmidt J.H., Wiener M.C., Tamm L.K. Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent. Protein Sci. 1999, 8:2065-2071.
    • (1999) Protein Sci. , vol.8 , pp. 2065-2071
    • Kleinschmidt, J.H.1    Wiener, M.C.2    Tamm, L.K.3
  • 91
    • 0033586718 scopus 로고    scopus 로고
    • Time-resolved distance determination by tryptophan fluorescence quenching: Probing intermediates in membrane protein folding
    • Kleinschmidt J.H., Tamm L.K. Time-resolved distance determination by tryptophan fluorescence quenching: Probing intermediates in membrane protein folding. Biochemistry 1999, 38:4996-5005.
    • (1999) Biochemistry , vol.38 , pp. 4996-5005
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 92
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a beta-barrel membrane protein: Kinetic evidence for a multi-step membrane insertion mechanism
    • Kleinschmidt J.H., Tamm L.K. Folding intermediates of a beta-barrel membrane protein: Kinetic evidence for a multi-step membrane insertion mechanism. Biochemistry 1996, 35:12993-13000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 93
    • 0033586795 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism
    • Kleinschmidt J.H., den Blaauwen T., Driessen A.J., Tamm L.K. Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism. Biochemistry 1999, 38:5006-5016.
    • (1999) Biochemistry , vol.38 , pp. 5006-5016
    • Kleinschmidt, J.H.1    den Blaauwen, T.2    Driessen, A.J.3    Tamm, L.K.4
  • 94
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a beta-barrel membrane protein
    • Surrey T., Jähnig F. Kinetics of folding and membrane insertion of a beta-barrel membrane protein. J. Biol. Chem. 1995, 270:28199-28203.
    • (1995) J. Biol. Chem. , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jähnig, F.2
  • 95
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of a membrane protein into a lipid bilayer
    • Surrey T., Jähnig F. Refolding and oriented insertion of a membrane protein into a lipid bilayer. Proc. Natl. Acad. Sci. USA 1992, 89:7457-7461.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 96
    • 34447135007 scopus 로고    scopus 로고
    • Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins
    • Hong H., Park S., Jimenez R.H., Rinehart D., Tamm L.K. Role of aromatic side chains in the folding and thermodynamic stability of integral membrane proteins. J. Am. Chem. Soc. 2007, 129:8320-8327.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 8320-8327
    • Hong, H.1    Park, S.2    Jimenez, R.H.3    Rinehart, D.4    Tamm, L.K.5
  • 97
    • 33750255413 scopus 로고    scopus 로고
    • Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
    • Hong H., Szabo G., Tamm L.K. Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening. Nat. Chem. Biol. 2006, 2:627-635.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 627-635
    • Hong, H.1    Szabo, G.2    Tamm, L.K.3
  • 98
    • 0034724567 scopus 로고    scopus 로고
    • High-resolution structure of the OmpA membrane domain
    • Pautsch A., Schulz G.E. High-resolution structure of the OmpA membrane domain. J. Mol. Biol. 2000, 298:273-282.
    • (2000) J. Mol. Biol. , vol.298 , pp. 273-282
    • Pautsch, A.1    Schulz, G.E.2
  • 99
    • 0022517918 scopus 로고
    • Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods
    • Vogel H., Jähnig F. Models for the structure of outer-membrane proteins of Escherichia coli derived from Raman spectroscopy and prediction methods. J. Mol. Biol. 1986, 190:191-199.
    • (1986) J. Mol. Biol. , vol.190 , pp. 191-199
    • Vogel, H.1    Jähnig, F.2
  • 100
    • 55549120907 scopus 로고    scopus 로고
    • Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • Burgess N.K., Dao T.P., Stanley A.M., Fleming K.G. Beta-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro. J. Biol. Chem. 2008, 283:26748-26758.
    • (2008) J. Biol. Chem. , vol.283 , pp. 26748-26758
    • Burgess, N.K.1    Dao, T.P.2    Stanley, A.M.3    Fleming, K.G.4
  • 102
    • 0025051457 scopus 로고
    • Quenching of tryptophan fluorescence by brominated phospholipid
    • Bolen E.J., Holloway P.W. Quenching of tryptophan fluorescence by brominated phospholipid. Biochemistry 1990, 29:9638-9643.
    • (1990) Biochemistry , vol.29 , pp. 9638-9643
    • Bolen, E.J.1    Holloway, P.W.2
  • 103
    • 0025249842 scopus 로고
    • Membrane protein folding and oligomerization: The two-stage model
    • Popot J.L., Engelman D.M. Membrane protein folding and oligomerization: The two-stage model. Biochemistry 1990, 29:4031-4037.
    • (1990) Biochemistry , vol.29 , pp. 4031-4037
    • Popot, J.L.1    Engelman, D.M.2
  • 105
    • 79959928058 scopus 로고    scopus 로고
    • Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers.
    • Moon C.P., Fleming K.G. Side-chain hydrophobicity scale derived from transmembrane protein folding into lipid bilayers. Proc. Natl. Acad. Sci. USA 2011, 108(25):10174-10177.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , Issue.25 , pp. 10174-10177
    • Moon, C.P.1    Fleming, K.G.2
  • 106
    • 80054719797 scopus 로고    scopus 로고
    • Overcoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers.
    • Moon C.P., Kwon S., Fleming K.G. Overcoming hysteresis to attain reversible equilibrium folding for outer membrane phospholipase A in phospholipid bilayers. J. Mol Biol. 2011, 413:484-494.
    • (2011) J. Mol Biol. , vol.413 , pp. 484-494
    • Moon, C.P.1    Kwon, S.2    Fleming, K.G.3
  • 107
    • 33749524795 scopus 로고    scopus 로고
    • Curvature elasticity and refolding of OmpA in large unilamellar vesicles
    • Pocanschi C.L., Patel G.J., Marsh D., Kleinschmidt J.H. Curvature elasticity and refolding of OmpA in large unilamellar vesicles. Biophys. J. 2006, 91:L75-L77.
    • (2006) Biophys. J. , vol.91
    • Pocanschi, C.L.1    Patel, G.J.2    Marsh, D.3    Kleinschmidt, J.H.4
  • 108
    • 57049130459 scopus 로고    scopus 로고
    • Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: Lessons from the transmembrane protein OmpA
    • Sanchez K.M., Gable J.E., Schlamadinger D.E., Kim J.E. Effects of tryptophan microenvironment, soluble domain, and vesicle size on the thermodynamics of membrane protein folding: Lessons from the transmembrane protein OmpA. Biochemistry 2008, 47:12844-12852.
    • (2008) Biochemistry , vol.47 , pp. 12844-12852
    • Sanchez, K.M.1    Gable, J.E.2    Schlamadinger, D.E.3    Kim, J.E.4
  • 109
    • 79951977489 scopus 로고    scopus 로고
    • Using tryptophan fluorescence to measure the stability of membrane proteins folded in liposomes.
    • Moon C.P., Fleming K.G. Using tryptophan fluorescence to measure the stability of membrane proteins folded in liposomes. Methods Enzymol. 2011, 492:189-211.
    • (2011) Methods Enzymol. , vol.492 , pp. 189-211
    • Moon, C.P.1    Fleming, K.G.2
  • 110
    • 33646727775 scopus 로고    scopus 로고
    • Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
    • Kleinschmidt J.H. Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers. Chem. Phys. Lipids 2006, 141:30-47.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 30-47
    • Kleinschmidt, J.H.1
  • 111
    • 33644644163 scopus 로고    scopus 로고
    • Insertion and assembly of membrane proteins via simulation
    • Bond P.J., Sansom M.S. Insertion and assembly of membrane proteins via simulation. J. Am. Chem. Soc. 2006, 128:2697-2704.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 2697-2704
    • Bond, P.J.1    Sansom, M.S.2
  • 113
    • 80052310851 scopus 로고    scopus 로고
    • The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.
    • Danoff E.J., Fleming K.G. The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel. Biophys. Chem. 2011, 159(1):194-204.
    • (2011) Biophys. Chem. , vol.159 , Issue.1 , pp. 194-204
    • Danoff, E.J.1    Fleming, K.G.2
  • 114
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar S.W., Kolter R. SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 1996, 178:1770-1773.
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 115
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D., Betton J.M., Raina S. New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol. Microbiol. 1996, 21:871-884.
    • (1996) Mol. Microbiol. , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 116
    • 33846234653 scopus 로고    scopus 로고
    • Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment
    • Ureta A.R., Endres R.G., Wingreen N.S., Silhavy T.J. Kinetic analysis of the assembly of the outer membrane protein LamB in Escherichia coli mutants each lacking a secretion or targeting factor in a different cellular compartment. J. Bacteriol. 2007, 189:446-454.
    • (2007) J. Bacteriol. , vol.189 , pp. 446-454
    • Ureta, A.R.1    Endres, R.G.2    Wingreen, N.S.3    Silhavy, T.J.4
  • 117
    • 17444392068 scopus 로고    scopus 로고
    • Characterization of six lipoproteins in the sigmaE regulon
    • Onufryk C., Crouch M.L., Fang F.C., Gross C.A. Characterization of six lipoproteins in the sigmaE regulon. J. Bacteriol. 2005, 187:4552-4561.
    • (2005) J. Bacteriol. , vol.187 , pp. 4552-4561
    • Onufryk, C.1    Crouch, M.L.2    Fang, F.C.3    Gross, C.A.4
  • 118
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • Ruiz N., Falcone B., Kahne D., Silhavy T.J. Chemical conditionality: A genetic strategy to probe organelle assembly. Cell 2005, 121:307-317.
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 119
    • 0030476750 scopus 로고    scopus 로고
    • SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins
    • Rouviere P.E., Gross C.A. SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, participates in the assembly of outer membrane porins. Genes Dev. 1996, 10:3170-3182.
    • (1996) Genes Dev. , vol.10 , pp. 3170-3182
    • Rouviere, P.E.1    Gross, C.A.2
  • 120
    • 33749593869 scopus 로고    scopus 로고
    • Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide
    • Charlson E.S., Werner J.N., Misra R. Differential effects of yfgL mutation on Escherichia coli outer membrane proteins and lipopolysaccharide. J. Bacteriol. 2006, 188:7186-7194.
    • (2006) J. Bacteriol. , vol.188 , pp. 7186-7194
    • Charlson, E.S.1    Werner, J.N.2    Misra, R.3
  • 121
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens S., Maier R., de Cock H., Schmid F.X., Gross C.A. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 2001, 20:285-294.
    • (2001) EMBO J. , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    de Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 122
    • 0035877593 scopus 로고    scopus 로고
    • Characterization of the Escherichia coli sigma E regulon
    • Dartigalongue C., Missiakas D., Raina S. Characterization of the Escherichia coli sigma E regulon. J. Biol. Chem. 2001, 276:20866-20875.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20866-20875
    • Dartigalongue, C.1    Missiakas, D.2    Raina, S.3
  • 123
    • 0035161025 scopus 로고    scopus 로고
    • Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli
    • Rizzitello A.E., Harper J.R., Silhavy T.J. Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli. J. Bacteriol. 2001, 183:6794-6800.
    • (2001) J. Bacteriol. , vol.183 , pp. 6794-6800
    • Rizzitello, A.E.1    Harper, J.R.2    Silhavy, T.J.3
  • 124
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schafer U., Beck K., Muller M. Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 1999, 274:24567-24574.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schafer, U.1    Beck, K.2    Muller, M.3
  • 125
    • 31144454629 scopus 로고    scopus 로고
    • Conserved and variable functions of the sigmaE stress response in related genomes
    • Rhodius V.A., Suh W.C., Nonaka G., West J., Gross C.A. Conserved and variable functions of the sigmaE stress response in related genomes. PLoS Biol. 2006, 4:e2.
    • (2006) PLoS Biol. , vol.4
    • Rhodius, V.A.1    Suh, W.C.2    Nonaka, G.3    West, J.4    Gross, C.A.5
  • 126
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins: Role of Skp in the biogenesis of outer membrane protein
    • De Cock H., Schafer U., Potgeter M., Demel R., Muller M., Tommassen J. Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins: Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 1999, 259:96-103.
    • (1999) Eur. J. Biochem. , vol.259 , pp. 96-103
    • De Cock, H.1    Schafer, U.2    Potgeter, M.3    Demel, R.4    Muller, M.5    Tommassen, J.6
  • 127
    • 35348966245 scopus 로고    scopus 로고
    • The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions
    • Qu J., Mayer C., Behrens S., Holst O., Kleinschmidt J.H. The trimeric periplasmic chaperone Skp of Escherichia coli forms 1:1 complexes with outer membrane proteins via hydrophobic and electrostatic interactions. J. Mol. Biol. 2007, 374:91-105.
    • (2007) J. Mol. Biol. , vol.374 , pp. 91-105
    • Qu, J.1    Mayer, C.2    Behrens, S.3    Holst, O.4    Kleinschmidt, J.H.5
  • 128
    • 42049111603 scopus 로고    scopus 로고
    • Physiological improvement to enhance Escherichia coli cell-surface display via reducing extracytoplasmic stress
    • Narayanan N., Chou C.P. Physiological improvement to enhance Escherichia coli cell-surface display via reducing extracytoplasmic stress. Biotechnol. Prog. 2008, 24:293-301.
    • (2008) Biotechnol. Prog. , vol.24 , pp. 293-301
    • Narayanan, N.1    Chou, C.P.2
  • 129
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • Levy R., Weiss R., Chen G., Iverson B.L., Georgiou G. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Protein Expr. Purif. 2001, 23:338-347.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 338-347
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.L.4    Georgiou, G.5
  • 130
    • 40849137556 scopus 로고    scopus 로고
    • A step-wise approach significantly enhances protein yield of a rationally-designed agonist antibody fragment in E. coli
    • Lin B., Renshaw M.W., Autote K., Smith L.M., Calveley P., Bowdish K.S., Frederickson S. A step-wise approach significantly enhances protein yield of a rationally-designed agonist antibody fragment in E. coli. Protein Expr. Purif. 2008, 59:55-63.
    • (2008) Protein Expr. Purif. , vol.59 , pp. 55-63
    • Lin, B.1    Renshaw, M.W.2    Autote, K.3    Smith, L.M.4    Calveley, P.5    Bowdish, K.S.6    Frederickson, S.7
  • 131
    • 0034761653 scopus 로고    scopus 로고
    • Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin
    • Mavrangelos C., Thiel M., Adamson P.J., Millard D.J., Nobbs S., Zola H., Nicholson I.C. Increased yield and activity of soluble single-chain antibody fragments by combining high-level expression and the Skp periplasmic chaperonin. Protein Expr. Purif. 2001, 23:289-295.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 289-295
    • Mavrangelos, C.1    Thiel, M.2    Adamson, P.J.3    Millard, D.J.4    Nobbs, S.5    Zola, H.6    Nicholson, I.C.7
  • 132
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann H., Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat. Biotechnol. 1998, 16:376-380.
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 133
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 2003, 278:9092-9099.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 134
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • Patel G.J., Behrens-Kneip S., Holst O., Kleinschmidt J.H. The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 2009, 48:10235-10245.
    • (2009) Biochemistry , vol.48 , pp. 10235-10245
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 135
    • 1842787813 scopus 로고    scopus 로고
    • The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization
    • Schlapschy M., Dommel M.K., Hadian K., Fogarasi M., Korndorfer I.P., Skerra A. The periplasmic E. coli chaperone Skp is a trimer in solution: Biophysical and preliminary crystallographic characterization. Biol. Chem. 2004, 385:137-143.
    • (2004) Biol. Chem. , vol.385 , pp. 137-143
    • Schlapschy, M.1    Dommel, M.K.2    Hadian, K.3    Fogarasi, M.4    Korndorfer, I.P.5    Skerra, A.6
  • 136
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton T.A., Sandoval C.M., Fowler C.A., Pardi A., Sousa M.C. The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. USA 2009, 106:1772-1777.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 137
    • 66649116274 scopus 로고    scopus 로고
    • Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp: A site-directed fluorescence study
    • Qu J., Behrens-Kneip S., Holst O., Kleinschmidt J.H. Binding regions of outer membrane protein A in complexes with the periplasmic chaperone Skp: A site-directed fluorescence study. Biochemistry 2009, 48:4926-4936.
    • (2009) Biochemistry , vol.48 , pp. 4926-4936
    • Qu, J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 138
    • 4744373535 scopus 로고    scopus 로고
    • Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture
    • Korndorfer I.P., Dommel M.K., Skerra A. Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat. Struct. Mol. Biol. 2004, 11:1015-1020.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 1015-1020
    • Korndorfer, I.P.1    Dommel, M.K.2    Skerra, A.3
  • 139
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • Walton T.A., Sousa M.C. Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 2004, 15:367-374.
    • (2004) Mol. Cell , vol.15 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 140
    • 0023035811 scopus 로고
    • An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export
    • Freudl R., Schwarz H., Stierhof Y.D., Gamon K., Hindennach I., Henning U. An outer membrane protein (OmpA) of Escherichia coli K-12 undergoes a conformational change during export. J. Biol. Chem. 1986, 261:11355-11361.
    • (1986) J. Biol. Chem. , vol.261 , pp. 11355-11361
    • Freudl, R.1    Schwarz, H.2    Stierhof, Y.D.3    Gamon, K.4    Hindennach, I.5    Henning, U.6
  • 142
    • 2642553745 scopus 로고    scopus 로고
    • Outer membrane proteins of pathogenic spirochetes
    • Cullen P.A., Haake D.A., Adler B. Outer membrane proteins of pathogenic spirochetes. FEMS Microbiol. Rev. 2004, 28:291-318.
    • (2004) FEMS Microbiol. Rev. , vol.28 , pp. 291-318
    • Cullen, P.A.1    Haake, D.A.2    Adler, B.3
  • 143
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • Hennecke G., Nolte J., Volkmer-Engert R., Schneider-Mergener J., Behrens S. The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition. J. Biol. Chem. 2005, 280:23540-23548.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 144
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • Bitto E., McKay D.B. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 2002, 10:1489-1498.
    • (2002) Structure , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 145
    • 1542571983 scopus 로고    scopus 로고
    • The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins
    • Bitto E., McKay D.B. The periplasmic molecular chaperone protein SurA binds a peptide motif that is characteristic of integral outer membrane proteins. J. Biol. Chem. 2003, 278:49316-49322.
    • (2003) J. Biol. Chem. , vol.278 , pp. 49316-49322
    • Bitto, E.1    McKay, D.B.2
  • 146
    • 34548851967 scopus 로고    scopus 로고
    • The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues
    • Xu X., Wang S., Hu Y.X., McKay D.B. The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues. J. Mol. Biol. 2007, 373:367-381.
    • (2007) J. Mol. Biol. , vol.373 , pp. 367-381
    • Xu, X.1    Wang, S.2    Hu, Y.X.3    McKay, D.B.4
  • 147
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R., Silhavy T.J. YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol. Microbiol. 2006, 61:151-164.
    • (2006) Mol. Microbiol. , vol.61 , pp. 151-164
    • Malinverni, J.C.1    Werner, J.2    Kim, S.3    Sklar, J.G.4    Kahne, D.5    Misra, R.6    Silhavy, T.J.7
  • 148
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • Robert V., Volokhina E.B., Senf F., Bos M.P., Van Gelder P., Tommassen J. Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol. 2006, 4:e377.
    • (2006) PLoS Biol. , vol.4
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 149
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie J.P., Sassoon N., Betton J.M. Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 2001, 39:199-210.
    • (2001) Mol. Microbiol. , vol.39 , pp. 199-210
    • Arie, J.P.1    Sassoon, N.2    Betton, J.M.3
  • 150
    • 0035816225 scopus 로고    scopus 로고
    • High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA
    • Ramm K., Pluckthun A. High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA. J. Mol. Biol. 2001, 310:485-498.
    • (2001) J. Mol. Biol. , vol.310 , pp. 485-498
    • Ramm, K.1    Pluckthun, A.2
  • 151
    • 0346366809 scopus 로고    scopus 로고
    • Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity
    • Saul F.A., Arie J.P., Vulliez-le Normand B., Kahn R., Betton J.M., Bentley G.A. Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 2004, 335:595-608.
    • (2004) J. Mol. Biol. , vol.335 , pp. 595-608
    • Saul, F.A.1    Arie, J.P.2    Vulliez-le Normand, B.3    Kahn, R.4    Betton, J.M.5    Bentley, G.A.6
  • 152
    • 0037187588 scopus 로고    scopus 로고
    • Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine
    • Krojer T., Garrido-Franco M., Huber R., Ehrmann M., Clausen T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 2002, 416:455-459.
    • (2002) Nature , vol.416 , pp. 455-459
    • Krojer, T.1    Garrido-Franco, M.2    Huber, R.3    Ehrmann, M.4    Clausen, T.5
  • 153
    • 45149106311 scopus 로고    scopus 로고
    • Structural basis for the regulated protease and chaperone function of DegP
    • Krojer T., Sawa J., Schafer E., Saibil H.R., Ehrmann M., Clausen T. Structural basis for the regulated protease and chaperone function of DegP. Nature 2008, 453:885-890.
    • (2008) Nature , vol.453 , pp. 885-890
    • Krojer, T.1    Sawa, J.2    Schafer, E.3    Saibil, H.R.4    Ehrmann, M.5    Clausen, T.6
  • 154
    • 0037214416 scopus 로고    scopus 로고
    • Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture
    • CastilloKeller M., Misra R. Protease-deficient DegP suppresses lethal effects of a mutant OmpC protein by its capture. J. Bacteriol. 2003, 185:148-154.
    • (2003) J. Bacteriol. , vol.185 , pp. 148-154
    • CastilloKeller, M.1    Misra, R.2
  • 156
    • 18844384961 scopus 로고    scopus 로고
    • Protein secretion in the absence of ATP: The autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review)
    • Thanassi D.G., Stathopoulos C., Karkal A., Li H. Protein secretion in the absence of ATP: The autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review). Mol. Membr. Biol. 2005, 22:63-72.
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 63-72
    • Thanassi, D.G.1    Stathopoulos, C.2    Karkal, A.3    Li, H.4
  • 157
    • 0042090321 scopus 로고    scopus 로고
    • Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential
    • Vandeputte-Rutten L., Bos M.P., Tommassen J., Gros P. Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential. J. Biol. Chem. 2003, 278(27):24825-24830.
    • (2003) J. Biol. Chem. , vol.278 , Issue.27 , pp. 24825-24830
    • Vandeputte-Rutten, L.1    Bos, M.P.2    Tommassen, J.3    Gros, P.4
  • 159
    • 0037133637 scopus 로고    scopus 로고
    • Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis
    • Prince S.M., Achtman M., Derrick J.P. Crystal structure of the OpcA integral membrane adhesin from Neisseria meningitidis. Proc. Natl. Acad. Sci. USA 2002, 99(6):3417-3421.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , Issue.6 , pp. 3417-3421
    • Prince, S.M.1    Achtman, M.2    Derrick, J.P.3
  • 160
    • 11144222920 scopus 로고    scopus 로고
    • Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: Dual modes of membrane anchoring and occluded cavity end
    • Akama H., Kanemaki M., Yoshimura M., Tsukihara T., Kashiwagi T., Yoneyama H., Narita S., Nakagawa A., Nakae T. Crystal structure of the drug discharge outer membrane protein, OprM, of Pseudomonas aeruginosa: Dual modes of membrane anchoring and occluded cavity end. J. Biol. Chem. 2004, 279(51):52816-52819.
    • (2004) J. Biol. Chem. , vol.279 , Issue.51 , pp. 52816-52819
    • Akama, H.1    Kanemaki, M.2    Yoshimura, M.3    Tsukihara, T.4    Kashiwagi, T.5    Yoneyama, H.6    Narita, S.7    Nakagawa, A.8    Nakae, T.9
  • 162
    • 70449533002 scopus 로고    scopus 로고
    • NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family
    • Wirth C., Condemine G., Boiteux C., Bernèche S., Schirmer T., Peneff C.M. NanC crystal structure, a model for outer-membrane channels of the acidic sugar-specific KdgM porin family. J. Mol. Biol. 2009, 394(4):718-731.
    • (2009) J. Mol. Biol. , vol.394 , Issue.4 , pp. 718-731
    • Wirth, C.1    Condemine, G.2    Boiteux, C.3    Bernèche, S.4    Schirmer, T.5    Peneff, C.M.6
  • 163
    • 77949323924 scopus 로고    scopus 로고
    • Crystal structure of a full-length autotransporter
    • van den Berg B. Crystal structure of a full-length autotransporter. J. Mol. Biol. 2010, 396(3):627-633.
    • (2010) J. Mol. Biol. , vol.396 , Issue.3 , pp. 627-633
    • van den Berg, B.1
  • 164
    • 47249160634 scopus 로고    scopus 로고
    • Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation
    • Hearn E.M., Patel D.R., van den Berg B. Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation. Proc. Natl. Acad. Sci. USA 2008, 105(25):8601-8606.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , Issue.25 , pp. 8601-8606
    • Hearn, E.M.1    Patel, D.R.2    van den Berg, B.3
  • 165
    • 0030447720 scopus 로고    scopus 로고
    • Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore
    • Song L., Hobaugh M.R., Shustak C., Cheley S., Bayley H., Gouaux J.E. Structure of staphylococcal alpha-hemolysin, a heptameric transmembrane pore. Science 1996, 274(5294):1859-1866.
    • (1996) Science , vol.274 , Issue.5294 , pp. 1859-1866
    • Song, L.1    Hobaugh, M.R.2    Shustak, C.3    Cheley, S.4    Bayley, H.5    Gouaux, J.E.6
  • 166
    • 33745727012 scopus 로고    scopus 로고
    • Crystal structure of the monomeric porin OmpG
    • Subbarao G.V., van den Berg B. Crystal structure of the monomeric porin OmpG. J. Mol. Biol. 2006, 360(4):750-759.
    • (2006) J. Mol. Biol. , vol.360 , Issue.4 , pp. 750-759
    • Subbarao, G.V.1    van den Berg, B.2
  • 167
    • 33747623998 scopus 로고    scopus 로고
    • Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation
    • Yildiz O., Vinothkumar K.R., Goswami P., Kühlbrandt W. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation. EMBO J. 2006, 25(15):3702-3713.
    • (2006) EMBO J. , vol.25 , Issue.15 , pp. 3702-3713
    • Yildiz, O.1    Vinothkumar, K.R.2    Goswami, P.3    Kühlbrandt, W.4
  • 168
    • 0026737314 scopus 로고
    • Structure of porin refined at 1.8Å resolution
    • Weiss M.S., Schulz G.E. Structure of porin refined at 1.8Å resolution. J. Mol. Biol. 1992, 227(2):493-509.
    • (1992) J. Mol. Biol. , vol.227 , Issue.2 , pp. 493-509
    • Weiss, M.S.1    Schulz, G.E.2
  • 169
    • 0028153088 scopus 로고
    • Refined structure of the porin from Rhodopseudomonas blastica: Comparison with the porin from Rhodobacter capsulatus
    • Kreusch A., Schulz G.E. Refined structure of the porin from Rhodopseudomonas blastica: Comparison with the porin from Rhodobacter capsulatus. J. Mol. Biol. 1994, 243(5):891-905.
    • (1994) J. Mol. Biol. , vol.243 , Issue.5 , pp. 891-905
    • Kreusch, A.1    Schulz, G.E.2
  • 170
    • 18744422713 scopus 로고    scopus 로고
    • Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure
    • Schmid B., Kromer M., Schulz G.E. Expression of porin from Rhodopseudomonas blastica in Escherichia coli inclusion bodies and folding into exact native structure. FEBS Lett. 1996, 381(1-2):111-114.
    • (1996) FEBS Lett. , vol.381 , Issue.1-2 , pp. 111-114
    • Schmid, B.1    Kromer, M.2    Schulz, G.E.3
  • 172
    • 0034665240 scopus 로고    scopus 로고
    • Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1Å resolution
    • Zeth K., Diederichs K., Welte W., Engelhardt H. Crystal structure of Omp32, the anion-selective porin from Comamonas acidovorans, in complex with a periplasmic peptide at 2.1Å resolution. Structure 2000, 8(9):981-992.
    • (2000) Structure , vol.8 , Issue.9 , pp. 981-992
    • Zeth, K.1    Diederichs, K.2    Welte, W.3    Engelhardt, H.4
  • 173
    • 33646354636 scopus 로고    scopus 로고
    • High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32
    • Zachariae U., Klühspies T., De S., Engelhardt H., Zeth K. High resolution crystal structures and molecular dynamics studies reveal substrate binding in the porin Omp32. J. Biol. Chem. 2006, 281(11):7413-7420.
    • (2006) J. Biol. Chem. , vol.281 , Issue.11 , pp. 7413-7420
    • Zachariae, U.1    Klühspies, T.2    De, S.3    Engelhardt, H.4    Zeth, K.5
  • 175
    • 49149127813 scopus 로고    scopus 로고
    • Crystal structures of the OmpF porin: Function in a colicin translocon
    • Yamashita E., Zhalnina M.V., Zakharov S.D., Sharma O., Cramer W.A. Crystal structures of the OmpF porin: Function in a colicin translocon. EMBO J. 2008, 27(15):2171-2180.
    • (2008) EMBO J. , vol.27 , Issue.15 , pp. 2171-2180
    • Yamashita, E.1    Zhalnina, M.V.2    Zakharov, S.D.3    Sharma, O.4    Cramer, W.A.5
  • 176
    • 33846113922 scopus 로고    scopus 로고
    • An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
    • Moraes T.F., Bains M., Hancock R.E., Strynadka N.C. An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nat. Struct. Mol. Biol. 2007, 14(1):85-87.
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , Issue.1 , pp. 85-87
    • Moraes, T.F.1    Bains, M.2    Hancock, R.E.3    Strynadka, N.C.4
  • 177
    • 0031557404 scopus 로고    scopus 로고
    • Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside
    • Meyer J.E., Hofnung M., Schulz G.E. Structure of maltoporin from Salmonella typhimurium ligated with a nitrophenyl-maltotrioside. J. Mol. Biol. 1997, 266(4):761-775.
    • (1997) J. Mol. Biol. , vol.266 , Issue.4 , pp. 761-775
    • Meyer, J.E.1    Hofnung, M.2    Schulz, G.E.3
  • 178
    • 46049091548 scopus 로고    scopus 로고
    • Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa
    • Biswas S., Mohammad M.M., Movileanu L., van den Berg B. Crystal structure of the outer membrane protein OpdK from Pseudomonas aeruginosa. Structure 2008, 16(7):1027-1035.
    • (2008) Structure , vol.16 , Issue.7 , pp. 1027-1035
    • Biswas, S.1    Mohammad, M.M.2    Movileanu, L.3    van den Berg, B.4
  • 180
  • 182
    • 63149140852 scopus 로고    scopus 로고
    • Use of an in-house approach to study the three-dimensional structures of various outer membrane proteins: Structure of the alcaligin outer membrane transporter FauA from Bordetella pertussis
    • Brillet K., Meksem A., Lauber E., Reimmann C., Cobessi D. Use of an in-house approach to study the three-dimensional structures of various outer membrane proteins: Structure of the alcaligin outer membrane transporter FauA from Bordetella pertussis. Acta Crystallogr. D Biol. Crystallogr. 2009, 65(Pt 4):326-331.
    • (2009) Acta Crystallogr. D Biol. Crystallogr. , vol.65 , Issue.PT 4 , pp. 326-331
    • Brillet, K.1    Meksem, A.2    Lauber, E.3    Reimmann, C.4    Cobessi, D.5
  • 184
    • 0033373495 scopus 로고    scopus 로고
    • Overexpression and refolding of an 80-kDa iron transporter from the outer membrane of Escherichia coli
    • Buchanan S.K. Overexpression and refolding of an 80-kDa iron transporter from the outer membrane of Escherichia coli. Biochem. Soc. Trans. 1999, 27(6):903-908.
    • (1999) Biochem. Soc. Trans. , vol.27 , Issue.6 , pp. 903-908
    • Buchanan, S.K.1
  • 185
    • 0034079929 scopus 로고    scopus 로고
    • Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA
    • Ferguson A.D., Braun V., Fiedler H.P., Coulton J.W., Diederichs K., Welte W. Crystal structure of the antibiotic albomycin in complex with the outer membrane transporter FhuA. Protein Sci. 2000, 9(5):956-963.
    • (2000) Protein Sci. , vol.9 , Issue.5 , pp. 956-963
    • Ferguson, A.D.1    Braun, V.2    Fiedler, H.P.3    Coulton, J.W.4    Diederichs, K.5    Welte, W.6
  • 186
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • Cobessi D., Celia H., Pattus F. Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J. Mol. Biol. 2005, 352(4):893-904.
    • (2005) J. Mol. Biol. , vol.352 , Issue.4 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 187
  • 188
    • 84882754916 scopus 로고    scopus 로고
    • Structure Determination of YiuR from Yersinia pestis
    • Noinaj N., et al. Structure Determination of YiuR from Yersinia pestis. Manuscript in preparation 2010.
    • (2010) Manuscript in preparation
    • Noinaj, N.1
  • 190
    • 77449152698 scopus 로고    scopus 로고
    • Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: Heme binding by an induced fit mechanism
    • Cobessi D., Meksem A., Brillet K. Structure of the heme/hemoglobin outer membrane receptor ShuA from Shigella dysenteriae: Heme binding by an induced fit mechanism. Proteins 2009, 78(2):286-294.
    • (2009) Proteins , vol.78 , Issue.2 , pp. 286-294
    • Cobessi, D.1    Meksem, A.2    Brillet, K.3
  • 191
    • 0032527831 scopus 로고    scopus 로고
    • A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli
    • Dartigalongue C., Raina S. A new heat-shock gene, ppiD, encodes a peptidyl-prolyl isomerase required for folding of outer membrane proteins in Escherichia coli. EMBO J. 1998, 17(14):3968-3980.
    • (1998) EMBO J. , vol.17 , Issue.14 , pp. 3968-3980
    • Dartigalongue, C.1    Raina, S.2
  • 192
    • 27744565064 scopus 로고    scopus 로고
    • Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli
    • Justice S.S., Hunstad D.A., Harper J.R., Duguay A.R., Pinkner J.S., Bann J., Frieden C., Silhavy T.J., Hultgren S.J. Periplasmic peptidyl prolyl cis-trans isomerases are not essential for viability, but SurA is required for pilus biogenesis in Escherichia coli. J. Bacteriol. 2005, 187(22):7680-7686.
    • (2005) J. Bacteriol. , vol.187 , Issue.22 , pp. 7680-7686
    • Justice, S.S.1    Hunstad, D.A.2    Harper, J.R.3    Duguay, A.R.4    Pinkner, J.S.5    Bann, J.6    Frieden, C.7    Silhavy, T.J.8    Hultgren, S.J.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.