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Volumn 12, Issue 2, 2011, Pages 123-128

Structure and function of BamE within the outer membrane and the β-barrel assembly machine

Author keywords

Bam complex; BamE; Omp85; outer membrane biogenesis; SmpA

Indexed keywords

BAME PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLGLYCEROL; UNCLASSIFIED DRUG;

EID: 79551577091     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2010.202     Document Type: Article
Times cited : (81)

References (32)
  • 1
    • 35348906348 scopus 로고    scopus 로고
    • Biogenesis of the gram-negative bacterial outer membrane
    • Bos MP, Robert V, Tommassen J (2007) Biogenesis of the gram-negative bacterial outer membrane. Annu Rev Microbiol 61: 191-214
    • (2007) Annu Rev Microbiol , vol.61 , pp. 191-214
    • Bos, M.P.1    Robert, V.2    Tommassen, J.3
  • 2
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu G, Delaglio F, Bax A (1999) Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR 13: 289-302
    • (1999) J Biomol NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 5
    • 0004757060 scopus 로고    scopus 로고
    • San Francisco, CA, USA: University of California
    • Goddard TD, Kneller DG (2004) SPARKY 3. San Francisco, CA, USA: University of California
    • (2004) SPARKY , pp. 3
    • Goddard, T.D.1    Kneller, D.G.2
  • 6
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • Guntert P (2004) Automated NMR structure calculation with CYANA. Methods Mol Biol 278: 353-378
    • (2004) Methods Mol Biol , vol.278 , pp. 353-378
    • Guntert, P.1
  • 7
    • 77952363712 scopus 로고    scopus 로고
    • Reconstitution of outer membrane protein assembly from purified components
    • Hagan CL, Kim S, Kahne D (2010) Reconstitution of outer membrane protein assembly from purified components. Science 328: 890-892
    • (2010) Science , vol.328 , pp. 890-892
    • Hagan, C.L.1    Kim, S.2    Kahne, D.3
  • 8
    • 0031571645 scopus 로고    scopus 로고
    • Determination of the kinetic parameters for phospholipase C (Bacillus cereus) on different phospholipid substrates using a chromogenic assay based on the quantitation of inorganic phosphate
    • Hergenrother PJ, Martin SF (1997) Determination of the kinetic parameters for phospholipase C (Bacillus cereus) on different phospholipid substrates using a chromogenic assay based on the quantitation of inorganic phosphate. Anal Biochem 251: 45-49
    • (1997) Anal Biochem , vol.251 , pp. 45-49
    • Hergenrother, P.J.1    Martin, S.F.2
  • 9
    • 0033824470 scopus 로고    scopus 로고
    • DaliLite workbench for protein structure comparison
    • Holm L, Park J (2000) DaliLite workbench for protein structure comparison. Bioinformatics 16: 566-567
    • (2000) Bioinformatics , vol.16 , pp. 566-567
    • Holm, L.1    Park, J.2
  • 10
    • 34548139422 scopus 로고    scopus 로고
    • Structure and function of an essential component of the outer membrane protein assembly machine
    • Kim S, Malinverni JC, Sliz P, Silhavy TJ, Harrison SC, Kahne D (2007) Structure and function of an essential component of the outer membrane protein assembly machine. Science 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
  • 12
    • 70449523240 scopus 로고    scopus 로고
    • Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli
    • Knowles TJ, McClelland DM, Rajesh S, Henderson IR, Overduin M (2009a) Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli. Biomol NMR Assign 3: 203-206
    • (2009) Biomol NMR Assign , vol.3 , pp. 203-206
    • Knowles, T.J.1    McClelland, D.M.2    Rajesh, S.3    Henderson, I.R.4    Overduin, M.5
  • 13
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: The role of the BAM complex in outer membrane protein assembly
    • Knowles TJ, Scott-Tucker A, Overduin M, Henderson IR (2009b) Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 7: 206-214
    • (2009) Nat Rev Microbiol , vol.7 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 14
    • 77957946859 scopus 로고    scopus 로고
    • Secondary structure and (1)H, (13)C and (15)N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli
    • Knowles TJ, Sridhar P, Rajesh S, Manoli E, Overduin M, Henderson IR (2010) Secondary structure and (1)H, (13)C and (15)N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli. Biomol NMR Assign 4: 179-181
    • (2010) Biomol NMR Assign , vol.4 , pp. 179-181
    • Knowles, T.J.1    Sridhar, P.2    Rajesh, S.3    Manoli, E.4    Overduin, M.5    Henderson, I.R.6
  • 15
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • 29-32
    • Koradi R, Billeter M, Wuthrich K (1996) MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph 14: 51-55, 29-32
    • (1996) J Mol Graph , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 16
  • 17
    • 34250159870 scopus 로고    scopus 로고
    • A set of BEST triple-resonance experiments for time-optimized protein resonance assignment
    • Lescop E, Schanda P, Brutscher B (2007) A set of BEST triple-resonance experiments for time-optimized protein resonance assignment. J Magn Reson 187: 163-169
    • (2007) J Magn Reson , vol.187 , pp. 163-169
    • Lescop, E.1    Schanda, P.2    Brutscher, B.3
  • 18
    • 0034919240 scopus 로고    scopus 로고
    • Automated assignment of ambiguous nuclear overhauser effects with ARIA
    • 0Donoghue SI, Nilges M (2001) Automated assignment of ambiguous nuclear overhauser effects with ARIA. Methods Enzymol 339: 71-90
    • (2001) Methods Enzymol , vol.339 , pp. 71-90
    • Linge, J.P.1    O'Donoghue, S.I.2    Nilges, M.3
  • 19
    • 33745202589 scopus 로고    scopus 로고
    • YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli
    • Malinverni JC, Werner J, Kim S, Sklar JG, Kahne D, Misra R, Silhavy TJ (2006) YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli. Mol Microbiol 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
  • 20
    • 4544384204 scopus 로고    scopus 로고
    • Lipoprotein trafficking in Escherichia coli
    • Narita S, Matsuyama S, Tokuda H (2004) Lipoprotein trafficking in Escherichia coli. Arch Microbiol 182: 1-6
    • (2004) Arch Microbiol , vol.182 , pp. 1-6
    • Narita, S.1    Matsuyama, S.2    Tokuda, H.3
  • 21
    • 0033020793 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA
    • Ochsner UA, Vasil AI, Johnson Z, Vasil ML (1999) Pseudomonas aeruginosa fur overlaps with a gene encoding a novel outer membrane lipoprotein, OmlA. J Bacteriol 181: 1099-1109
    • (1999) J Bacteriol , vol.181 , pp. 1099-1109
    • Ochsner, U.A.1    Vasil, A.I.2    Johnson, Z.3    Vasil, M.L.4
  • 22
    • 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 GJ, Behrens-Kneip S, Holst O, Kleinschmidt JH (2009) The periplasmic chaperone Skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 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
  • 23
    • 17444385981 scopus 로고    scopus 로고
    • Chemical conditionality: A genetic strategy to probe organelle assembly
    • Ruiz N, Falcone B, Kahne D, Silhavy TJ (2005) Chemical conditionality: a genetic strategy to probe organelle assembly. Cell 121: 307-317
    • (2005) Cell , vol.121 , pp. 307-317
    • Ruiz, N.1    Falcone, B.2    Kahne, D.3    Silhavy, T.J.4
  • 24
    • 33746082442 scopus 로고    scopus 로고
    • Speeding up three-dimensional protein NMR experiments to a few minutes
    • Schanda P, Van Melckebeke H, Brutscher B (2006) Speeding up three-dimensional protein NMR experiments to a few minutes. J Am Chem Soc 128: 9042-9043
    • (2006) J Am Chem Soc , vol.128 , pp. 9042-9043
    • Schanda, P.1    Van Melckebeke, H.2    Brutscher, B.3
  • 25
    • 34547512065 scopus 로고    scopus 로고
    • Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli
    • Sklar JG, Wu T, Gronenberg LS, Malinverni JC, Kahne D, Silhavy TJ (2007) Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli. Proc Natl Acad Sci USA 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
  • 26
    • 0030583720 scopus 로고    scopus 로고
    • Vanadate is a potent competitive inhibitor of phospholipase C from Bacillus cereus
    • Tan CA, Roberts MF (1996) Vanadate is a potent competitive inhibitor of phospholipase C from Bacillus cereus. Biochim Biophys Acta 1298: 58-68
    • (1996) Biochim Biophys Acta , vol.1298 , pp. 58-68
    • Tan, C.A.1    Roberts, M.F.2
  • 27
    • 44349166323 scopus 로고    scopus 로고
    • The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction
    • Vanini MM, Spisni A, Sforca ML, Pertinhez TA, Benedetti CE (2008) The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein-protein interaction. Proteins 71: 2051-2064
    • (2008) Proteins , vol.71 , pp. 2051-2064
    • Vanini, M.M.1    Spisni, A.2    Sforca, M.L.3    Pertinhez, T.A.4    Benedetti, C.E.5
  • 28
    • 0042565977 scopus 로고    scopus 로고
    • Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane
    • Vanounou S, Parola AH, Fishov I (2003) Phosphatidylethanolamine and phosphatidylglycerol are segregated into different domains in bacterial membrane. A study with pyrene-labelled phospholipids. Mol Microbiol 49: 1067-1079
    • (2003) A Study with Pyrene-labelled Phospholipids. Mol Microbiol , vol.49 , pp. 1067-1079
    • Vanounou, S.1    Parola, A.H.2    Fishov, I.3
  • 29
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J (2003) Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 299: 262-265
    • (2003) Science , vol.299 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 31
    • 39749086276 scopus 로고    scopus 로고
    • Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry
    • Vuong P, Bennion D, Mantei J, Frost D, Misra R (2008) Analysis of YfgL and YaeT interactions through bioinformatics, mutagenesis, and biochemistry. J Bacteriol 190: 1507-1517
    • (2008) J Bacteriol , vol.190 , pp. 1507-1517
    • Vuong, P.1    Bennion, D.2    Mantei, J.3    Frost, D.4    Misra, R.5
  • 32
    • 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 TJ, Kahne D (2005) Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 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


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