메뉴 건너뛰기




Volumn 287, Issue 49, 2012, Pages 41044-41052

Structural basis for outer membrane sugar uptake in pseudomonads

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE RESIDUE; EXTRACELLULAR LOOPS; GLUCOSE MOLECULES; GRAM-NEGATIVE BACTERIA; NEGATIVE CHARGE; OUTER MEMBRANE; PSEUDOMONAS PUTIDA F1; SIDE-CHAINS; SMALL MOLECULES; STRUCTURAL BASIS; X RAY CRYSTAL STRUCTURES;

EID: 84870354012     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.408518     Document Type: Article
Times cited : (37)

References (37)
  • 1
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido, H. (2003) Molecular basis of bacterial outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67, 593-656
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 2
    • 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., and van den Berg, B. (2009) Transmembrane passage of hydrophobic compounds through a protein channel wall. Nature 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
  • 3
    • 33846113922 scopus 로고    scopus 로고
    • An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane
    • DOI 10.1038/nsmb1189, PII NSMB1189
    • Moraes, T. F., Bains, M., Hancock, R. E., and Strynadka, N. C. (2007) An arginine ladder in OprP mediates phosphate-specific transfer across the outer membrane. Nat. Struct. Mol. Biol. 14, 85-87 (Pubitemid 46067427)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.1 , pp. 85-87
    • Moraes, T.F.1    Bains, M.2    Hancock, R.E.W.3    Strynadka, N.C.J.4
  • 4
    • 0027959128 scopus 로고
    • A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis
    • Klebba, P. E., Hofnung, M., and Charbit, A. (1994) A model of maltodextrin transport through the sugar-specific porin, LamB, based on deletion analysis. EMBO J. 13, 4670-4675 (Pubitemid 24310218)
    • (1994) EMBO Journal , vol.13 , Issue.19 , pp. 4670-4675
    • Klebba, P.E.1    Hofnung, M.2    Charbit, A.3
  • 5
    • 0030871753 scopus 로고    scopus 로고
    • Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin
    • DOI 10.1016/S0923-2508(97)83868-5
    • Klebba, P. E., Newton, S. M., Charbit, A., Michel, V., Perrin, D., and Hofnung, M. (1997) Further genetic analysis of the C-terminal external loop region in Escherichia coli maltoporin. Res Microbiol. 148, 375-387 (Pubitemid 27314918)
    • (1997) Research in Microbiology , vol.148 , Issue.5 , pp. 375-387
    • Klebba, P.E.1    Newton, S.M.C.2    Charbit, A.3    Michel, V.4    Perrin, D.5    Hofnung, M.6
  • 6
    • 0028946962 scopus 로고
    • Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution
    • Schirmer, T., Keller, T. A., Wang, Y. F., and Rosenbusch, J. P. (1995) Structural basis for sugar translocation through maltoporin channels at 3.1 Å resolution. Science 267, 512-514
    • (1995) Science , vol.267 , pp. 512-514
    • Schirmer, T.1    Keller, T.A.2    Wang, Y.F.3    Rosenbusch, J.P.4
  • 7
    • 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., and Schirmer, T. (1996) Crystal structures of various maltooligosaccharides bound to maltoporin reveal a specific sugar translocation pathway. Structure 4, 127-134 (Pubitemid 126658976)
    • (1996) Structure , vol.4 , Issue.2 , pp. 127-134
    • Dutzler, R.1    Wang, Y.-F.2    Rizkallah, P.J.3    Rosenbusch, J.P.4    Schirmer, T.5
  • 8
    • 0034733718 scopus 로고    scopus 로고
    • Sugar transport through maltoporin of Escherichia coli: Role of polar tracks
    • DOI 10.1074/jbc.M000268200
    • Dumas, F., Koebnik, R., Winterhalter, M., and Van Gelder, P. (2000) Sugar transport through maltoporin of Escherichia coli. Role of polar tracks. J. Biol. Chem. 275, 19747-19751 (Pubitemid 30441574)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.26 , pp. 19747-19751
    • Dumas, F.1    Koebnik, R.2    Winterhalter, M.3    Van Gelder, P.4
  • 9
    • 33644903806 scopus 로고    scopus 로고
    • Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa
    • Tamber, S., Ochs, M. M., and Hancock, R. E. (2006) Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa. J. Bacteriol. 188, 45-54
    • (2006) J. Bacteriol. , vol.188 , pp. 45-54
    • Tamber, S.1    Ochs, M.M.2    Hancock, R.E.3
  • 12
    • 69249147800 scopus 로고    scopus 로고
    • Regulation of glucose metabolism in Pseudomonas. The phosphorylative branch and Entner-Doudoroff enzymes are regulated by a repressor containing a sugar isomerase domain
    • Daddaoua A., Krell T., and Ramos J. L. (2009) Regulation of glucose metabolism in Pseudomonas. The phosphorylative branch and Entner-Doudoroff enzymes are regulated by a repressor containing a sugar isomerase domain. J. Biol. Chem. 284, 21360-21368
    • (2009) J. Biol. Chem. , vol.284 , pp. 21360-21368
    • Daddaoua, A.1    Krell, T.2    Ramos, J.L.3
  • 13
    • 0019190802 scopus 로고
    • Protein D1: A glucose-inducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa
    • DOI 10.1016/0378-1097(80)90079-8
    • Hancock, R. E. W., and Carey A. M. (1980) Protein D1. A glucose inducible, pore-forming protein from the outer membrane of Pseudomonas aeruginosa. FEMS Microbiol. Lett. 8, 105-109 (Pubitemid 10062205)
    • (1980) FEMS Microbiology Letters , vol.8 , Issue.2 , pp. 105-109
    • Hancock, R.E.W.1    Carey, A.M.2
  • 14
    • 0026344024 scopus 로고
    • Purification of glucose-inducible outer membrane protein OprB of Pseudomonas putida and reconstitution of glucose-specific pores
    • Saravolac, E. G., Taylor, N. F., Benz, R., and Hancock, R. E. (1991) Purification of glucose-inducible outer membrane protein OprB of Pseudomonas putida and reconstitution of glucose-specific pores. J. Bacteriol. 173, 4970-4976
    • (1991) J. Bacteriol. , vol.173 , pp. 4970-4976
    • Saravolac, E.G.1    Taylor, N.F.2    Benz, R.3    Hancock, R.E.4
  • 15
    • 0029056666 scopus 로고
    • The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa
    • Wylie, J. L., and Worobec, E. A. (1995) The OprB porin plays a central role in carbohydrate uptake in Pseudomonas aeruginosa. J. Bacteriol. 177, 3021-3026
    • (1995) J. Bacteriol. , vol.177 , pp. 3021-3026
    • Wylie, J.L.1    Worobec, E.A.2
  • 16
    • 0031783488 scopus 로고    scopus 로고
    • Channel specificity and secondary structure of the glucose-inducible porins of Pseudomonas spp.
    • Adewoye, L. O., Tschetter, L., O'Neil, J., and Worobec, E. A. (1998) Channel specificity and secondary structure of the glucose-inducible porins of Pseudomonas spp. J. Bioenerg. Biomembr. 30, 257-267 (Pubitemid 28405167)
    • (1998) Journal of Bioenergetics and Biomembranes , vol.30 , Issue.3 , pp. 257-267
    • Adewoye, L.O.1    Tschetter, L.2    O'Neil, J.3    Worobec, E.A.4
  • 17
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter
    • Guzman, L. M., Belin, D., Carson, M. J., and Beckwith, J. (1995) Tight regulation, modulation, and high level expression by vectors containing the arabinose PBAD promoter. J. Bacteriol. 177, 4121-4130
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 19
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • DOI 10.1006/jmbi.1993.1012
    • Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L., and Clardy, J. (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124 (Pubitemid 23037917)
    • (1993) Journal of Molecular Biology , vol.229 , Issue.1 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 20
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 0020522392 scopus 로고
    • Porin channels in Escherichia coli: Studies with β-lactams in intact cells
    • Nikaido, H., Rosenberg, E. Y., and Foulds, J. (1983) Porin channels in Escherichia coli. Studies with β-lactams in intact cells. J. Bacteriol. 153, 232-240 (Pubitemid 13119860)
    • (1983) Journal of Bacteriology , vol.153 , Issue.1 , pp. 232-240
    • Nikaido, H.1    Rosenberg, E.Y.2    Foulds, J.3
  • 25
    • 3242883431 scopus 로고    scopus 로고
    • PRED-TMBB: A web server for predicting the topology of β-barrel outer membrane proteins
    • DOI 10.1093/nar/gkh417
    • Bagos, P. G., Liakopoulos, T. D., Spyropoulos, I. C., and Hamodrakas, S. J. (2004) PRED-TMBB. A web server for predicting the topology of β-barrel outer membrane proteins. Nucleic Acids Res. 32, W400-W404 (Pubitemid 38997367)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Bagos, P.G.1    Liakopoulos, T.D.2    Spyropoulos, I.C.3    Hamodrakas, S.J.4
  • 26
    • 79955756112 scopus 로고    scopus 로고
    • Repression of the glucose-inducible outer-membrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86
    • Shrivastava, R., Basu, B., Godbole, A., Mathew, M. K., Apte, S. K., and Phale, P. S. (2011) Repression of the glucose-inducible outer-membrane protein OprB during utilization of aromatic compounds and organic acids in Pseudomonas putida CSV86. Microbiology 157, 1531-1540
    • (2011) Microbiology , vol.157 , pp. 1531-1540
    • Shrivastava, R.1    Basu, B.2    Godbole, A.3    Mathew, M.K.4    Apte, S.K.5    Phale, P.S.6
  • 27
    • 0032506042 scopus 로고    scopus 로고
    • Stability of trimeric OmpF porin: The contributions of the latching loop L2
    • DOI 10.1021/bi981215c
    • Phale, P. S., Philippsen, A., Kiefhaber, T., Koebnik, R., Phale, V. P., Schirmer, T., and Rosenbusch, J. P. (1998) Stability of trimeric OmpF porin. The contributions of the latching loop L2. Biochemistry 37, 15663-15670 (Pubitemid 28524736)
    • (1998) Biochemistry , vol.37 , Issue.45 , pp. 15663-15670
    • Phale, P.S.1    Philippsen, A.2    Kiefhaber, T.3    Koebnik, R.4    Phale, V.P.5    Schirmer, T.6    Rosenbusch, J.P.7
  • 28
    • 0029835190 scopus 로고    scopus 로고
    • Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo
    • Van Gelder, P., and Tommassen, J. (1996) Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo. J. Bacteriol. 178, 5320-5322 (Pubitemid 26293096)
    • (1996) Journal of Bacteriology , vol.178 , Issue.17 , pp. 5320-5322
    • Van Gelder, P.1    Tommassen, J.2
  • 29
    • 0031716791 scopus 로고    scopus 로고
    • Architecture of β-barrel membrane proteins: Analysis of trimeric porins
    • Seshadri, K., Garemyr, R., Wallin, E., von Heijne, G., and Elofsson, A. (1998) Architecture of β-barrel membrane proteins. Analysis of trimeric porins. Protein Sci. 7, 2026-2032 (Pubitemid 28432444)
    • (1998) Protein Science , vol.7 , Issue.9 , pp. 2026-2032
    • Seshadri, K.1    Garemyr, R.2    Wallin, E.3    Von Heijne, G.4    Elofsson, A.5
  • 30
    • 77954288774 scopus 로고    scopus 로고
    • Dali server. Conservation mapping in 3D
    • Holm, L., and Rosenström, P. (2010) Dali server. Conservation mapping in 3D. Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenström, P.2
  • 31
    • 0023650005 scopus 로고
    • Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E. coli outer membrane
    • Dargent, B., Rosenbusch, J., and Pattus, F. (1987) Selectivity for maltose and maltodextrins of maltoporin, a pore-forming protein of E. coli outer membrane. FEBS Lett. 220, 136-142
    • (1987) FEBS Lett. , vol.220 , pp. 136-142
    • Dargent, B.1    Rosenbusch, J.2    Pattus, F.3
  • 32
    • 0025273178 scopus 로고
    • LamB (maltoporin) of Salmonella typhimurium. Isolation, purification and comparison of sugar binding with LamB of Escherichia coli
    • Schülein K., and Benz R. (1990) LamB (maltoporin) of Salmonella typhimurium. Isolation, purification and comparison of sugar binding with LamB of Escherichia coli. Mol. Microbiol. 4, 625-632
    • (1990) Mol. Microbiol. , vol.4 , pp. 625-632
    • Schülein, K.1    Benz, R.2
  • 33
    • 0026545214 scopus 로고
    • Investigation of the selectivity of maltoporin channels using mutant LamB proteins. Mutations changing the maltodextrin binding site
    • Benz, R., Francis, G., Nakae, T., and Ferenci, T. (1992) Investigation of the selectivity of maltoporin channels using mutant LamB proteins. Mutations changing the maltodextrin binding site. Biochim. Biophys. Acta. 1104, 299-307
    • (1992) Biochim. Biophys. Acta. , vol.1104 , pp. 299-307
    • Benz, R.1    Francis, G.2    Nakae, T.3    Ferenci, T.4
  • 34
    • 0022515322 scopus 로고
    • Pore formation by LamB of Escherichia coli in lipid bilayer membranes
    • Benz, R., Schmid, A., Nakae, T., and Vos-Scheperkeuter, G. H. (1986) Pore formation by LamB of Escherichia coli in lipid bilayer membranes. J. Bacteriol. 165, 978-986 (Pubitemid 16071434)
    • (1986) Journal of Bacteriology , vol.165 , Issue.3 , pp. 978-986
    • Benz, R.1    Schmid, A.2    Nakae, T.3    Vos-Scheperkeuter, G.H.4
  • 35
    • 0031985785 scopus 로고    scopus 로고
    • Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose
    • DOI 10.1038/nsb0198-37
    • Forst, D., Welte, W., Wacker, T., and Diederichs, K. (1998) Structure of the sucrose-specific porin ScrY from Salmonella typhimurium and its complex with sucrose. Nat. Struct. Biol. 5, 37-46 (Pubitemid 28048975)
    • (1998) Nature Structural Biology , vol.5 , Issue.1 , pp. 37-46
    • Forst, D.1    Welte, W.2    Wacker, T.3    Diederichs, K.4
  • 37
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: An automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • DOI 10.1093/nar/gkh381
    • Dolinsky, T. J., Nielsen, J. E., McCammon, J. A., and Baker, N. A. (2004) (2004) PDB2PQR. An automated pipeline for the setup, execution, and analysis of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res. 32, W665-W667 (Pubitemid 38997419)
    • (2004) Nucleic Acids Research , vol.32 , Issue.WEB SERVER ISS.
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.