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Volumn 1808, Issue 1, 2011, Pages 287-297

The prediction and characterization of YshA, an unknown outer-membrane protein from Salmonella typhimurium

Author keywords

Beta barrel; Outer membrane protein; Salmonella; Structure prediction

Indexed keywords

OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN YSHA; UNCLASSIFIED DRUG;

EID: 78649763562     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.09.008     Document Type: Article
Times cited : (12)

References (47)
  • 1
    • 0041428149 scopus 로고    scopus 로고
    • The versatile β-barrel membrane protein
    • W.C. Wimley The versatile β-barrel membrane protein Curr. Opin. Struct. Biol. 13 2003 404 411
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 404-411
    • Wimley, W.C.1
  • 2
    • 0031740601 scopus 로고    scopus 로고
    • Hydrophobic interactions of peptides with membrane interfaces
    • S.H. White, and W.C. Wimley Hydrophobic interactions of peptides with membrane interfaces Biochim. Biophys. Acta 1376 1998 339 352
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 339-352
    • White, S.H.1    Wimley, W.C.2
  • 3
    • 0035812599 scopus 로고    scopus 로고
    • Energetics, stability, and prediction of transmembrane helices
    • S. Jayasinghe, K. Hristova, and S.H. White Energetics, stability, and prediction of transmembrane helices J. Mol. Biol. 312 2001 927 934
    • (2001) J. Mol. Biol. , vol.312 , pp. 927-934
    • Jayasinghe, S.1    Hristova, K.2    White, S.H.3
  • 5
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • S.H. White, and W.C. Wimley Membrane protein folding and stability: physical principles Annu. Rev. Biophys. Biomol. Struct. 28 1999 319 365
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 6
    • 0036147641 scopus 로고    scopus 로고
    • Toward genomic identification of β-barrel membrane proteins: Composition and architecture of known structures
    • W.C. Wimley Toward genomic identification of β-barrel membrane proteins: composition and architecture of known structures Protein Sci. 11 2002 301 312
    • (2002) Protein Sci. , vol.11 , pp. 301-312
    • Wimley, W.C.1
  • 7
    • 77955411469 scopus 로고    scopus 로고
    • A highly accurate statistical approach for the prediction of transmembrane β-barrels
    • Oxford, England
    • T.C. Freeman, Jr., W.C. Wimley, A highly accurate statistical approach for the prediction of transmembrane β-barrels, Bioinformatics (Oxford, England) 26 (2010) 1965-1974.
    • (2010) Bioinformatics , vol.26 , pp. 1965-1974
    • Freeman Jr., T.C.1    Wimley, W.C.2
  • 8
    • 0034669205 scopus 로고    scopus 로고
    • Protein folding in the periplasm in the absence of primary oxidant DsbA: Modulation of redox potential in periplasmic space via OmpL porin
    • C. Dartigalongue, H. Nikaido, and S. Raina Protein folding in the periplasm in the absence of primary oxidant DsbA: modulation of redox potential in periplasmic space via OmpL porin EMBO J. 19 2000 5980 5988
    • (2000) EMBO J. , vol.19 , pp. 5980-5988
    • Dartigalongue, C.1    Nikaido, H.2    Raina, S.3
  • 9
    • 0037390403 scopus 로고    scopus 로고
    • The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli
    • A.A. Sardesai, P. Genevaux, F. Schwager, D. Ang, and C. Georgopoulos The OmpL porin does not modulate redox potential in the periplasmic space of Escherichia coli EMBO J. 22 2003 1461 1466
    • (2003) EMBO J. , vol.22 , pp. 1461-1466
    • Sardesai, A.A.1    Genevaux, P.2    Schwager, F.3    Ang, D.4    Georgopoulos, C.5
  • 10
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • A.P. Pugsley The complete general secretory pathway in Gram-negative bacteria Microbiol. Rev. 57 1993 50 108
    • (1993) Microbiol. Rev. , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 12
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • D.P. Chimento, A.K. Mohanty, R.J. Kadner, and M.C. Wiener Substrate-induced transmembrane signaling in the cobalamin transporter BtuB Nat. Struct. Biol. 10 2003 394 401
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 13
    • 0016678144 scopus 로고
    • Maltose transport in Escherichia coli K-12: Involvement of the bacteriophage lambda receptor
    • S. Szmelcman, and M. Hofnung Maltose transport in Escherichia coli K-12: involvement of the bacteriophage lambda receptor J. Bacteriol. 124 1975 112 118
    • (1975) J. Bacteriol. , vol.124 , pp. 112-118
    • Szmelcman, S.1    Hofnung, M.2
  • 14
    • 55549120907 scopus 로고    scopus 로고
    • β-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro
    • N.K. Burgess, T.P. Dao, A.M. Stanley, and K.G. Fleming β-barrel proteins that reside in the Escherichia coli outer membrane in vivo demonstrate varied folding behavior in vitro J. Biol. Chem. 283 2008 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
  • 15
    • 0025081330 scopus 로고
    • Refolding of an integral membrane protein, OmpA of Escherichia coli
    • K. Dornmair, H. Kiefer, and F. Jahnig Refolding of an integral membrane protein, OmpA of Escherichia coli J. Biol. Chem. 265 1990 18907 18911
    • (1990) J. Biol. Chem. , vol.265 , pp. 18907-18911
    • Dornmair, K.1    Kiefer, H.2    Jahnig, F.3
  • 16
    • 0032832765 scopus 로고    scopus 로고
    • Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent
    • J.H. Kleinschmidt, M.C. Wiener, and L.K. Tamm Outer membrane protein A of E. coli folds into detergent micelles, but not in the presence of monomeric detergent Protein Sci. 8 1999 2065 2071
    • (1999) Protein Sci. , vol.8 , pp. 2065-2071
    • Kleinschmidt, J.H.1    Wiener, M.C.2    Tamm, L.K.3
  • 17
    • 0032532698 scopus 로고    scopus 로고
    • Characterization of a heat modifiable protein, Escherichia coli outer membrane protein OmpA in binary surfactant system of sodium dodecyl sulfate and octylglucoside
    • S. Ohnishi, K. Kameyama, and T. Takagi Characterization of a heat modifiable protein, Escherichia coli outer membrane protein OmpA in binary surfactant system of sodium dodecyl sulfate and octylglucoside Biochim. Biophys. Acta 1375 1998 101 109
    • (1998) Biochim. Biophys. Acta , vol.1375 , pp. 101-109
    • Ohnishi, S.1    Kameyama, K.2    Takagi, T.3
  • 18
    • 38349016735 scopus 로고    scopus 로고
    • Two-step folding of recombinant mitochondrial porin in detergent
    • D.C. Bay, J.D. O'Neil, and D.A. Court Two-step folding of recombinant mitochondrial porin in detergent Biophys. J. 94 2008 457 468
    • (2008) Biophys. J. , vol.94 , pp. 457-468
    • Bay, D.C.1    O'Neil, J.D.2    Court, D.A.3
  • 19
    • 0242669988 scopus 로고    scopus 로고
    • Conformational change in elastase following complexation with alpha1-proteinase inhibitor: A CD investigation
    • J.A. Bousquet, J. Duranton, Y. Mely, and J.G. Bieth Conformational change in elastase following complexation with alpha1-proteinase inhibitor: a CD investigation Biochem. J. 370 2003 345 349
    • (2003) Biochem. J. , vol.370 , pp. 345-349
    • Bousquet, J.A.1    Duranton, J.2    Mely, Y.3    Bieth, J.G.4
  • 20
    • 0035575842 scopus 로고    scopus 로고
    • Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding
    • S. Ohnishi, and K. Kameyama Escherichia coli OmpA retains a folded structure in the presence of sodium dodecyl sulfate due to a high kinetic barrier to unfolding Biochim. Biophys. Acta 1515 2001 159 166
    • (2001) Biochim. Biophys. Acta , vol.1515 , pp. 159-166
    • Ohnishi, S.1    Kameyama, K.2
  • 21
    • 0025301439 scopus 로고
    • Protein secondary structure and circular dichroism: A practical guide
    • W.C. Johnson Jr. Protein secondary structure and circular dichroism: a practical guide Proteins 7 1990 205 214
    • (1990) Proteins , vol.7 , pp. 205-214
    • Johnson Jr., W.C.1
  • 22
    • 0030949437 scopus 로고    scopus 로고
    • Bio-Beads: An efficient strategy for two-dimensional crystallization of membrane proteins
    • J.L. Rigaud, G. Mosser, J.J. Lacapere, A. Olofsson, D. Levy, and J.L. Ranck Bio-Beads: an efficient strategy for two-dimensional crystallization of membrane proteins J. Struct. Biol. 118 1997 226 235
    • (1997) J. Struct. Biol. , vol.118 , pp. 226-235
    • Rigaud, J.L.1    Mosser, G.2    Lacapere, J.J.3    Olofsson, A.4    Levy, D.5    Ranck, J.L.6
  • 23
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • H. Hong, and L.K. Tamm Elastic coupling of integral membrane protein stability to lipid bilayer forces Proc. Natl Acad. Sci. USA 101 2004 4065 4070
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 24
    • 0019287336 scopus 로고
    • Nonspecific and specific diffusion channels in the outer membrane of Escherichia coli
    • H. Nikaido, M. Luckey, and E.Y. Rosenberg Nonspecific and specific diffusion channels in the outer membrane of Escherichia coli J. Supramol. Struct. 13 1980 305 313
    • (1980) J. Supramol. Struct. , vol.13 , pp. 305-313
    • Nikaido, H.1    Luckey, M.2    Rosenberg, E.Y.3
  • 25
    • 0025968741 scopus 로고
    • Identification and characterization of porins in Pseudomonas aeruginosa
    • H. Nikaido, K. Nikaido, and S. Harayama Identification and characterization of porins in Pseudomonas aeruginosa J. Biol. Chem. 266 1991 770 779
    • (1991) J. Biol. Chem. , vol.266 , pp. 770-779
    • Nikaido, H.1    Nikaido, K.2    Harayama, S.3
  • 26
    • 0037164693 scopus 로고    scopus 로고
    • Estimation of the radius of the pores formed by the Bacillus thuringiensis Cry1C delta-endotoxin in planar lipid bilayers
    • O. Peyronnet, B. Nieman, F. Genereux, V. Vachon, R. Laprade, and J.L. Schwartz Estimation of the radius of the pores formed by the Bacillus thuringiensis Cry1C delta-endotoxin in planar lipid bilayers Biochim. Biophys. Acta 1567 2002 113 122
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 113-122
    • Peyronnet, O.1    Nieman, B.2    Genereux, F.3    Vachon, V.4    Laprade, R.5    Schwartz, J.L.6
  • 27
    • 0000815976 scopus 로고
    • Determination of the effective hydrodynamic radii of small molecules by viscometry
    • S.G. Schultz, and A.K. Solomon Determination of the effective hydrodynamic radii of small molecules by viscometry J. Gen. Physiol. 44 1961 1189 1199
    • (1961) J. Gen. Physiol. , vol.44 , pp. 1189-1199
    • Schultz, S.G.1    Solomon, A.K.2
  • 28
    • 69149083388 scopus 로고    scopus 로고
    • Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins
    • H. Naveed, R. Jackups Jr., and J. Liang Predicting weakly stable regions, oligomerization state, and protein-protein interfaces in transmembrane domains of outer membrane proteins Proc. Natl Acad. Sci. USA 106 2009 12735 12740
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 12735-12740
    • Naveed, H.1    Jackups Jr., R.2    Liang, J.3
  • 29
  • 30
    • 34250187443 scopus 로고    scopus 로고
    • The role of a hydrogen bonding network in the transmembrane β-barrel OMPLA
    • A.M. Stanley, and K.G. Fleming The role of a hydrogen bonding network in the transmembrane β-barrel OMPLA J. Mol. Biol. 370 2007 912 924
    • (2007) J. Mol. Biol. , vol.370 , pp. 912-924
    • Stanley, A.M.1    Fleming, K.G.2
  • 31
    • 0037040884 scopus 로고    scopus 로고
    • The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family
    • N. Blot, C. Berrier, N. Hugouvieux-Cotte-Pattat, A. Ghazi, and G. Condemine The oligogalacturonate-specific porin KdgM of Erwinia chrysanthemi belongs to a new porin family J. Biol. Chem. 277 2002 7936 7944
    • (2002) J. Biol. Chem. , vol.277 , pp. 7936-7944
    • Blot, N.1    Berrier, C.2    Hugouvieux-Cotte-Pattat, N.3    Ghazi, A.4    Condemine, G.5
  • 32
    • 14644401707 scopus 로고    scopus 로고
    • Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli
    • G. Condemine, C. Berrier, J. Plumbridge, and A. Ghazi Function and expression of an N-acetylneuraminic acid-inducible outer membrane channel in Escherichia coli J. Bacteriol. 187 2005 1959 1965
    • (2005) J. Bacteriol. , vol.187 , pp. 1959-1965
    • Condemine, G.1    Berrier, C.2    Plumbridge, J.3    Ghazi, A.4
  • 33
    • 55849140478 scopus 로고    scopus 로고
    • Identification of a bile-induced exopolysaccharide required for Salmonella biofilm formation on gallstone surfaces
    • R.W. Crawford, D.L. Gibson, W.W. Kay, and J.S. Gunn Identification of a bile-induced exopolysaccharide required for Salmonella biofilm formation on gallstone surfaces Infect. Immun. 76 2008 5341 5349
    • (2008) Infect. Immun. , vol.76 , pp. 5341-5349
    • Crawford, R.W.1    Gibson, D.L.2    Kay, W.W.3    Gunn, J.S.4
  • 34
    • 33751094307 scopus 로고    scopus 로고
    • Salmonella produces an O-antigen capsule regulated by AgfD and important for environmental persistence
    • D.L. Gibson, A.P. White, S.D. Snyder, S. Martin, C. Heiss, P. Azadi, M. Surette, and W.W. Kay Salmonella produces an O-antigen capsule regulated by AgfD and important for environmental persistence J. Bacteriol. 188 2006 7722 7730
    • (2006) J. Bacteriol. , vol.188 , pp. 7722-7730
    • Gibson, D.L.1    White, A.P.2    Snyder, S.D.3    Martin, S.4    Heiss, C.5    Azadi, P.6    Surette, M.7    Kay, W.W.8
  • 35
    • 0034816414 scopus 로고    scopus 로고
    • Overexpression, refolding, and purification of the histidine-tagged outer membrane efflux protein OprM of Pseudomonas aeruginosa
    • F. Charbonnier, T. Kohler, J.C. Pechere, and A. Ducruix Overexpression, refolding, and purification of the histidine-tagged outer membrane efflux protein OprM of Pseudomonas aeruginosa Protein Expr. Purif. 23 2001 121 127
    • (2001) Protein Expr. Purif. , vol.23 , pp. 121-127
    • Charbonnier, F.1    Kohler, T.2    Pechere, J.C.3    Ducruix, A.4
  • 36
    • 0242663865 scopus 로고    scopus 로고
    • Separation methods in the analysis of protein membrane complexes
    • Y. Kashino Separation methods in the analysis of protein membrane complexes J. Chromatogr. 797 2003 191 216
    • (2003) J. Chromatogr. , vol.797 , pp. 191-216
    • Kashino, Y.1
  • 37
    • 0041743087 scopus 로고    scopus 로고
    • Folding of DsbB in mixed micelles: A kinetic analysis of the stability of a bacterial membrane protein
    • D.E. Otzen Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein J. Mol. Biol. 330 2003 641 649
    • (2003) J. Mol. Biol. , vol.330 , pp. 641-649
    • Otzen, D.E.1
  • 38
    • 0033082712 scopus 로고    scopus 로고
    • A method for the purification and refolding of a recombinant form of the nontypeable Haemophilus influenzae P5 outer membrane protein fused to polyhistidine
    • D.C. Webb, and A.W. Cripps A method for the purification and refolding of a recombinant form of the nontypeable Haemophilus influenzae P5 outer membrane protein fused to polyhistidine Protein Expr. Purif. 15 1999 1 7
    • (1999) Protein Expr. Purif. , vol.15 , pp. 1-7
    • Webb, D.C.1    Cripps, A.W.2
  • 39
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • S.M. Singh, and A.K. Panda Solubilization and refolding of bacterial inclusion body proteins J. Biosci. Bioeng. 99 2005 303 310
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 40
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the β-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • J.H. Kleinschmidt, and L.K. Tamm Secondary and tertiary structure formation of the β-barrel membrane protein OmpA is synchronized and depends on membrane thickness J. Mol. Biol. 324 2002 319 330
    • (2002) J. Mol. Biol. , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 41
    • 0028785347 scopus 로고
    • Kinetics of folding and membrane insertion of a β-barrel membrane protein
    • T. Surrey, and F. Jahnig Kinetics of folding and membrane insertion of a β-barrel membrane protein J. Biol. Chem. 270 1995 28199 28203
    • (1995) J. Biol. Chem. , vol.270 , pp. 28199-28203
    • Surrey, T.1    Jahnig, F.2
  • 42
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • T.H. Bayburt, and S.G. Sligar Membrane protein assembly into Nanodiscs FEBS Lett. 584 2010 1721 1727
    • (2010) FEBS Lett. , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 44
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • V. Robert, E.B. Volokhina, F. Senf, M.P. Bos, P. Van Gelder, and J. Tommassen Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif PLoS Biol. 4 2006 e377
    • (2006) PLoS Biol. , vol.4 , pp. 377
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 45
    • 0036216078 scopus 로고    scopus 로고
    • Partitioning of differently sized poly(ethylene glycol)s into OmpF porin
    • T.K. Rostovtseva, E.M. Nestorovich, and S.M. Bezrukov Partitioning of differently sized poly(ethylene glycol)s into OmpF porin Biophys. J. 82 2002 160 169
    • (2002) Biophys. J. , vol.82 , pp. 160-169
    • Rostovtseva, T.K.1    Nestorovich, E.M.2    Bezrukov, S.M.3
  • 47
    • 33750508962 scopus 로고    scopus 로고
    • Functional assay of Salmonella typhi OmpC using reconstituted large unilamellar vesicles: A general method for characterization of outer membrane proteins
    • N. Sundara Baalaji, M.K. Mathew, and S. Krishnaswamy Functional assay of Salmonella typhi OmpC using reconstituted large unilamellar vesicles: a general method for characterization of outer membrane proteins Biochimie 88 2006 1419 1424
    • (2006) Biochimie , vol.88 , pp. 1419-1424
    • Sundara Baalaji, N.1    Mathew, M.K.2    Krishnaswamy, S.3


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