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Volumn 1614, Issue 2, 2003, Pages 201-210

Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB

Author keywords

Bacterium; Energization; Molecular modeling; Motility; Outer membrane transport; Proton channel

Indexed keywords

EXBB PROTEIN; ION CHANNEL; PROTEIN; PROTEIN EXBD; PROTEIN MOTA; PROTEIN MOTB; PROTEIN TONB; UNCLASSIFIED DRUG;

EID: 0041704803     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2736(03)00176-7     Document Type: Article
Times cited : (44)

References (85)
  • 1
    • 0028822933 scopus 로고
    • How bacteria sense and swim
    • Blair D.F. How bacteria sense and swim. Annu. Rev. Microbiol. 49:1995;489-522.
    • (1995) Annu. Rev. Microbiol. , vol.49 , pp. 489-522
    • Blair, D.F.1
  • 2
    • 0032478505 scopus 로고    scopus 로고
    • The turn of the screw: The bacterial flagellar motor
    • DeRosier D.J. The turn of the screw: the bacterial flagellar motor. Cell. 93:1998;17-20.
    • (1998) Cell , vol.93 , pp. 17-20
    • DeRosier, D.J.1
  • 3
    • 0027048626 scopus 로고
    • Genetics and biogenesis of bacterial flagella
    • Macnab R.M. Genetics and biogenesis of bacterial flagella. Annu. Rev. Genet. 26:1992;131-158.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 131-158
    • Macnab, R.M.1
  • 5
    • 0017835741 scopus 로고
    • The proton pump is a molecular engine of motile bacteria
    • Glagolev A.N., Skulachev V.P. The proton pump is a molecular engine of motile bacteria. Nature (Lond.). 272:1978;280-282.
    • (1978) Nature (Lond.) , vol.272 , pp. 280-282
    • Glagolev, A.N.1    Skulachev, V.P.2
  • 6
    • 0016219080 scopus 로고
    • Chemomechanical coupling without ATP: The source of energy for motility and chemotaxis in bacteria
    • Larsen S.H., Adler J., Gargus J.J., Hogg R.W. Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria. Proc. Natl. Acad. Sci. U. S. A. 71:1974;1239-1243.
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 1239-1243
    • Larsen, S.H.1    Adler, J.2    Gargus, J.J.3    Hogg, R.W.4
  • 7
    • 0000266432 scopus 로고
    • Bacterial flagellar motors and osmoelectric molecular rotation by an axially transmembrane well and turnstile mechanism
    • Mitchell P. Bacterial flagellar motors and osmoelectric molecular rotation by an axially transmembrane well and turnstile mechanism. FEBS Lett. 176:1984;287-294.
    • (1984) FEBS Lett. , vol.176 , pp. 287-294
    • Mitchell, P.1
  • 8
    • 0025718616 scopus 로고
    • Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli
    • Stolz B., Berg H.C. Evidence for interactions between MotA and MotB, torque-generating elements of the flagellar motor of Escherichia coli. J. Bacteriol. 173:1991;7033-7037.
    • (1991) J. Bacteriol. , vol.173 , pp. 7033-7037
    • Stolz, B.1    Berg, H.C.2
  • 9
    • 0032568636 scopus 로고    scopus 로고
    • Electrostatic interactions between rotor and stator in the bacterial flagellar motor
    • Zhou J., Lloyd S.A., Blair D.F. Electrostatic interactions between rotor and stator in the bacterial flagellar motor. Proc. Natl. Acad. Sci. U. S. A. 95:1998;6436-6441.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6436-6441
    • Zhou, J.1    Lloyd, S.A.2    Blair, D.F.3
  • 10
    • 0032744789 scopus 로고    scopus 로고
    • +-driven components can rotate Vibrio polar flagella by using sodium ions
    • +-driven components can rotate Vibrio polar flagella by using sodium ions. J. Bacteriol. 181:1999;6332-6338.
    • (1999) J. Bacteriol. , vol.181 , pp. 6332-6338
    • Asai, Y.1    Kawagishi, I.2    Sockett, R.E.3    Homma, M.4
  • 11
    • 0033985494 scopus 로고    scopus 로고
    • Cysteine-scanning mutagenesis of the periplasmic loop regions of PomA, a putative channel component of the sodium-driven flagellar motor in Vibrio alginolyticus
    • Asai Y., Shoji T., Kawagishi I., Homma M. Cysteine-scanning mutagenesis of the periplasmic loop regions of PomA, a putative channel component of the sodium-driven flagellar motor in Vibrio alginolyticus. J. Bacteriol. 182:2000;1001-1007.
    • (2000) J. Bacteriol. , vol.182 , pp. 1001-1007
    • Asai, Y.1    Shoji, T.2    Kawagishi, I.3    Homma, M.4
  • 12
    • 0033984762 scopus 로고    scopus 로고
    • Insertional inactivation of genes encoding components of the sodium-type flagellar motor and switch of Vibrio parahaemolyticus
    • Boles B.R., McCarter L.L. Insertional inactivation of genes encoding components of the sodium-type flagellar motor and switch of Vibrio parahaemolyticus. J. Bacteriol. 182:2000;1035-1045.
    • (2000) J. Bacteriol. , vol.182 , pp. 1035-1045
    • Boles, B.R.1    McCarter, L.L.2
  • 13
    • 0021037132 scopus 로고
    • +-driven flagellar motors of an alkalophilic Bacillus strain YN-1
    • +-driven flagellar motors of an alkalophilic Bacillus strain YN-1. J. Biol. Chem. 258:1983;10577-10581.
    • (1983) J. Biol. Chem. , vol.258 , pp. 10577-10581
    • Hirota, N.1    Imae, Y.2
  • 15
    • 0034051670 scopus 로고    scopus 로고
    • +-driven polar flagellar motor component of Vibrio alginolyticus
    • +-driven polar flagellar motor component of Vibrio alginolyticus. J. Biol. Chem. 275:2000;5718-5722.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5718-5722
    • Sato, K.1    Homma, M.2
  • 17
    • 0034677671 scopus 로고    scopus 로고
    • Mot protein assembly into the bacterial flagellum: A model based on mutational analysis of the motB gene
    • Van Way S.M., Hosking E.R., Braun T.F., Manson M.D. Mot protein assembly into the bacterial flagellum: a model based on mutational analysis of the motB gene. J. Mol. Biol. 297:2000;7-24.
    • (2000) J. Mol. Biol. , vol.297 , pp. 7-24
    • Van Way, S.M.1    Hosking, E.R.2    Braun, T.F.3    Manson, M.D.4
  • 18
    • 0034828107 scopus 로고    scopus 로고
    • Polar flagellar motility of the Vibrionaceae
    • McCarter L.L. Polar flagellar motility of the Vibrionaceae. Microbiol. Mol. Biol. Rev. 65:2001;445-462.
    • (2001) Microbiol. Mol. Biol. Rev. , vol.65 , pp. 445-462
    • McCarter, L.L.1
  • 19
    • 0025058346 scopus 로고
    • The MotA protein of E. coli is a proton-conducting component of the flagellar motor
    • Blair D.F., Berg H.C. The MotA protein of E. coli is a proton-conducting component of the flagellar motor. Cell. 60:1990;439-449.
    • (1990) Cell , vol.60 , pp. 439-449
    • Blair, D.F.1    Berg, H.C.2
  • 20
    • 0026068420 scopus 로고
    • Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction
    • Blair D.F., Berg H.C. Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction. J. Mol. Biol. 221:1991;1433-1442.
    • (1991) J. Mol. Biol. , vol.221 , pp. 1433-1442
    • Blair, D.F.1    Berg, H.C.2
  • 21
    • 0033000388 scopus 로고    scopus 로고
    • Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli
    • Braun T.F., Poulson S., Gully J.B., Empey J.C., Van Way S., Putnam A., Blair D.F. Function of proline residues of MotA in torque generation by the flagellar motor of Escherichia coli. J. Bacteriol. 181:1999;3542-3551.
    • (1999) J. Bacteriol. , vol.181 , pp. 3542-3551
    • Braun, T.F.1    Poulson, S.2    Gully, J.B.3    Empey, J.C.4    Van Way, S.5    Putnam, A.6    Blair, D.F.7
  • 22
    • 0031944413 scopus 로고    scopus 로고
    • Function of protonatable residues in the flagellar motor of Escherichia coli: A critical role for Asp32 of MotB
    • Zhou J., Sharp L.L., Tang H.L., Lloyd S.A., Billings S., Braun T.F., Blair D.F. Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp32 of MotB. J. Bacteriol. 180:1998;2729-2735.
    • (1998) J. Bacteriol. , vol.180 , pp. 2729-2735
    • Zhou, J.1    Sharp, L.L.2    Tang, H.L.3    Lloyd, S.A.4    Billings, S.5    Braun, T.F.6    Blair, D.F.7
  • 24
    • 0021611311 scopus 로고
    • Gene sequence and predicted amino acid sequence of the motA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli
    • Dean G.E., Macnab R.M., Stader J., Matsumura D., Burke C. Gene sequence and predicted amino acid sequence of the motA protein, a membrane-associated protein required for flagellar rotation in Escherichia coli. J. Bacteriol. 159:1984;991-999.
    • (1984) J. Bacteriol. , vol.159 , pp. 991-999
    • Dean, G.E.1    Macnab, R.M.2    Stader, J.3    Matsumura, D.4    Burke, C.5
  • 26
    • 0022531430 scopus 로고
    • Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane
    • Stader J., Matsumura P., Vacante D., Dean G.E., Macnab R.M. Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane. J. Bacteriol. 166:1986;244-252.
    • (1986) J. Bacteriol. , vol.166 , pp. 244-252
    • Stader, J.1    Matsumura, P.2    Vacante, D.3    Dean, G.E.4    Macnab, R.M.5
  • 27
    • 0024286468 scopus 로고
    • Bacterial motility: Membrane topology of the Escherichia coli MotB protein
    • Chun S.Y., Parkinson J.S. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science. 239:1988;276-278.
    • (1988) Science , vol.239 , pp. 276-278
    • Chun, S.Y.1    Parkinson, J.S.2
  • 28
    • 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
    • DeMot 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. 12:1994;333-334.
    • (1994) Mol. Microbiol. , vol.12 , pp. 333-334
    • DeMot, R.1    Vanderleyden, J.2
  • 30
    • 0343603660 scopus 로고    scopus 로고
    • A functional/phylogenetic classification system for transmembrane solute transporters
    • Saier M.H. Jr. A functional/phylogenetic classification system for transmembrane solute transporters. Microbiol. Mol. Biol. Rev. 64:2000;354-411.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 354-411
    • Saier M.H., Jr.1
  • 32
    • 0035980241 scopus 로고    scopus 로고
    • + channels in the stator complex
    • + channels in the stator complex. Biochemistry. 40:2001;13051-13059.
    • (2001) Biochemistry , vol.40 , pp. 13051-13059
    • Braun, T.F.1    Blair, D.F.2
  • 33
    • 0034733660 scopus 로고    scopus 로고
    • +-driven polar flagellar motor of Vibrio alginolyticus
    • +-driven polar flagellar motor of Vibrio alginolyticus. J. Biol. Chem. 275:2000;20223-20228.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20223-20228
    • Sato, K.1    Homma, M.2
  • 34
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • Cascales E., Lloubès R., Sturgis J.N. The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Mol. Microbiol. 42:2001;795-807.
    • (2001) Mol. Microbiol. , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubès, R.2    Sturgis, J.N.3
  • 35
    • 0037783318 scopus 로고    scopus 로고
    • Tracing pathways of transport protein evolution
    • Saier M.H. Jr. Tracing pathways of transport protein evolution. Mol. Microbiol. 48:2003;1145-1156.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1145-1156
    • Saier M.H., Jr.1
  • 36
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima S., Blair D.F. Conformational change in the stator of the bacterial flagellar motor. Biochemistry. 40:2001;13041-13050.
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2
  • 37
    • 0030893908 scopus 로고    scopus 로고
    • Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes
    • Biswas G.D., Anderson J.E., Sparling P.F. Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes. Mol. Microbiol. 24:1997;169-179.
    • (1997) Mol. Microbiol. , vol.24 , pp. 169-179
    • Biswas, G.D.1    Anderson, J.E.2    Sparling, P.F.3
  • 38
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun V., Braun M. Iron transport and signaling in Escherichia coli. FEBS Lett. 529:2002;78-85.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 39
    • 0028954576 scopus 로고
    • Utilization of transferrin-bound iron by Haemophilus influenzae requires an intact tonB gene
    • Jarosik G.P., MacIver I., Cope L.D., Hansen E.J. Utilization of transferrin-bound iron by Haemophilus influenzae requires an intact tonB gene. Infect. Immun. 63:1995;710-713.
    • (1995) Infect. Immun. , vol.63 , pp. 710-713
    • Jarosik, G.P.1    MacIver, I.2    Cope, L.D.3    Hansen, E.J.4
  • 40
    • 0031018882 scopus 로고    scopus 로고
    • Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in Neisseriae
    • Stojiljkovic I., Srinivasan N. Neisseria meningitidis tonB, exbB, and exbD genes: ton-dependent utilization of protein-bound iron in Neisseriae. J. Bacteriol. 179:1997;805-812.
    • (1997) J. Bacteriol. , vol.179 , pp. 805-812
    • Stojiljkovic, I.1    Srinivasan, N.2
  • 41
    • 0028363283 scopus 로고
    • A functional tonB gene is required for both utilization of heme and virulence expression by Haemophilus influenzae Type B
    • Jarosik G.P., Sanders J.D., Cope L.D., Muller-Eberhard U., Hansen E.J. A functional tonB gene is required for both utilization of heme and virulence expression by Haemophilus influenzae Type B. Infect. Immun. 62:1994;2470-2477.
    • (1994) Infect. Immun. , vol.62 , pp. 2470-2477
    • Jarosik, G.P.1    Sanders, J.D.2    Cope, L.D.3    Muller-Eberhard, U.4    Hansen, E.J.5
  • 42
    • 0031033423 scopus 로고    scopus 로고
    • Haem iron-transport system in enterohaemorrhagic Escherichia coli O157:H7
    • Torres A.G., Payne S.M. Haem iron-transport system in enterohaemorrhagic Escherichia coli O157:H7. Mol. Microbiol. 23:1997;825-833.
    • (1997) Mol. Microbiol. , vol.23 , pp. 825-833
    • Torres, A.G.1    Payne, S.M.2
  • 43
    • 0032832385 scopus 로고    scopus 로고
    • Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin, as iron sources
    • Nicholson M.L., Beall B. Disruption of tonB in Bordetella bronchiseptica and Bordetella pertussis prevents utilization of ferric siderophores, haemin and haemoglobin, as iron sources. Microbiology. 145:1999;2453-2461.
    • (1999) Microbiology , vol.145 , pp. 2453-2461
    • Nicholson, M.L.1    Beall, B.2
  • 45
    • 0036786885 scopus 로고    scopus 로고
    • Structure and dynamics of the β-barrel of the membrane transporter BtuB by site-directed spin labeling
    • Fanucci G.E., Cadieux N., Piedmont C.A., Kadner R.J., Cafiso D.S. Structure and dynamics of the β-barrel of the membrane transporter BtuB by site-directed spin labeling. Biochemistry. 41:2002;11543-11551.
    • (2002) Biochemistry , vol.41 , pp. 11543-11551
    • Fanucci, G.E.1    Cadieux, N.2    Piedmont, C.A.3    Kadner, R.J.4    Cafiso, D.S.5
  • 46
    • 0034878780 scopus 로고    scopus 로고
    • Involvement of the TonB system in tolerance to solvents and drugs in Pseudomonas putida DOT-T1E
    • Godoy P., Ramos-González M.I., Ramos J.L. Involvement of the TonB system in tolerance to solvents and drugs in Pseudomonas putida DOT-T1E. J. Bacteriol. 183:2001;5285-5292.
    • (2001) J. Bacteriol. , vol.183 , pp. 5285-5292
    • Godoy, P.1    Ramos-González, M.I.2    Ramos, J.L.3
  • 47
    • 0036208645 scopus 로고    scopus 로고
    • Differential effects of mutations in tonB1 on intrinsic multidrug resistance and iron acquisition in Pseudomonas aeruginosa
    • Zhao Q., Poole K. Differential effects of mutations in tonB1 on intrinsic multidrug resistance and iron acquisition in Pseudomonas aeruginosa. J. Bacteriol. 184:2002;2045-2049.
    • (2002) J. Bacteriol. , vol.184 , pp. 2045-2049
    • Zhao, Q.1    Poole, K.2
  • 48
    • 0034767924 scopus 로고    scopus 로고
    • Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm
    • Journet L., Bouveret E., Rigal A., Lloubes R., Lazdunski C., Bénédetti H. Import of colicins across the outer membrane of Escherichia coli involves multiple protein interactions in the periplasm. Mol. Microbiol. 42:2001;331-344.
    • (2001) Mol. Microbiol. , vol.42 , pp. 331-344
    • Journet, L.1    Bouveret, E.2    Rigal, A.3    Lloubes, R.4    Lazdunski, C.5    Bénédetti, H.6
  • 49
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD dependent receptor proteins
    • Braun V. Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD dependent receptor proteins. FEMS Microbiol. Rev. 16:1995;295-307.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 50
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs P.I., Myers P.S., Postle K. Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers. J. Bacteriol. 180:1998;6031-6038.
    • (1998) J. Bacteriol. , vol.180 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 51
    • 0032991467 scopus 로고    scopus 로고
    • Proton motive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen R.A., Thomas M.G., Postle K. Proton motive force, ExbB and ligand-bound FepA drive conformational changes in TonB. Mol. Microbiol. 31:1999;1809-1824.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 52
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs P.I., Larsen R.A., Postle K. Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol. Microbiol. 44:2002;271-281.
    • (2002) Mol. Microbiol. , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 53
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson A.D., Hofmann E., Coulton J.W., Diederichs K., Welte W. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science. 282:1998;2215-2220.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 54
    • 0032774018 scopus 로고    scopus 로고
    • The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability
    • Lazzaroni J.C., Germon J.C., Ray M.-C., Vianney A. The Tol proteins of Escherichia coli and their involvement in the uptake of biomolecules and outer membrane stability. FEMS Microbiol. Lett. 177:1999;191-197.
    • (1999) FEMS Microbiol. Lett. , vol.177 , pp. 191-197
    • Lazzaroni, J.C.1    Germon, J.C.2    Ray, M.-C.3    Vianney, A.4
  • 55
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • Letain T.E., Postle T.E. TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli. Mol. Microbiol. 24:1997;271-283.
    • (1997) Mol. Microbiol. , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, T.E.2
  • 56
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • Larsen R.A., Foster-Hartnett D., McIntosh M.A., Postle K. Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions. J. Bacteriol. 179:1997;3213-3221.
    • (1997) J. Bacteriol. , vol.179 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 57
    • 0030680156 scopus 로고    scopus 로고
    • Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor fhua promotes interaction with the energy-transducing protein TonB
    • Moeck G.S., Coulton J.W., Postle K. Cell envelope signaling in Escherichia coli. Ligand binding to the ferrichrome-iron receptor fhua promotes interaction with the energy-transducing protein TonB. J. Biol. Chem. 272:1997;28391-28397.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28391-28397
    • Moeck, G.S.1    Coulton, J.W.2    Postle, K.3
  • 58
    • 0019230249 scopus 로고
    • 12 in Escherichia coli. Some observations on the roles of the gene products of BtuC and TonB
    • 12 in Escherichia coli. Some observations on the roles of the gene products of BtuC and TonB. J. Biol. Chem. 255:1980;4313-4319.
    • (1980) J. Biol. Chem. , vol.255 , pp. 4313-4319
    • Reynolds, P.R.1    Mottur, G.P.2    Bradbeer, C.3
  • 59
    • 0026533769 scopus 로고
    • In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide
    • Tuckman M., Osburne M.S. In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide. J. Bacteriol. 174:1992;320-323.
    • (1992) J. Bacteriol. , vol.174 , pp. 320-323
    • Tuckman, M.1    Osburne, M.S.2
  • 60
    • 0027466914 scopus 로고
    • Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli
    • Kampfenkel K., Braun V. Topology of the ExbB protein in the cytoplasmic membrane of Escherichia coli. J. Biol. Chem. 268:1993;6050-6057.
    • (1993) J. Biol. Chem. , vol.268 , pp. 6050-6057
    • Kampfenkel, K.1    Braun, V.2
  • 61
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • Kampfenkel K., Braun V. Membrane topology of the Escherichia coli ExbD protein. J. Bacteriol. 174:1992;5485-5487.
    • (1992) J. Bacteriol. , vol.174 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 62
    • 0029117190 scopus 로고
    • Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability
    • Ahmer B.M.M., Thomas M.G., Larsen R.A., Postle K. Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability. J. Bacteriol. 177:1995;4742-4747.
    • (1995) J. Bacteriol. , vol.177 , pp. 4742-4747
    • Ahmer, B.M.M.1    Thomas, M.G.2    Larsen, R.A.3    Postle, K.4
  • 63
    • 0027280517 scopus 로고
    • The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
    • Bradbeer C. The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli. J. Bacteriol. 175:1993;3146-3150.
    • (1993) J. Bacteriol. , vol.175 , pp. 3146-3150
    • Bradbeer, C.1
  • 64
    • 0027282061 scopus 로고
    • Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
    • Skare J.T., Ahmer B.M.M., Seachord C.L., Darveau R.P., Postle K. Energy transduction between membranes. TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA. J. Biol. Chem. 268:1993;16302-16308.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 65
    • 0029913411 scopus 로고    scopus 로고
    • Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity
    • Braun V., Gaisser S., Herrmann C., Kampfenkel K., Killmann H., Traub I. Energy-coupled transport across the outer membrane of Escherichia coli: ExbB binds ExbD and TonB in vitro, and leucine 132 in the periplasmic region and aspartate 25 in the transmembrane region are important for ExbD activity. J. Bacteriol. 178:1996;2836-2845.
    • (1996) J. Bacteriol. , vol.178 , pp. 2836-2845
    • Braun, V.1    Gaisser, S.2    Herrmann, C.3    Kampfenkel, K.4    Killmann, H.5    Traub, I.6
  • 66
    • 0027168466 scopus 로고
    • Activity domains of the TonB protein
    • Traub I., Gaisser S., Braun V. Activity domains of the TonB protein. Mol. Microbiol. 8:1993;409-423.
    • (1993) Mol. Microbiol. , vol.8 , pp. 409-423
    • Traub, I.1    Gaisser, S.2    Braun, V.3
  • 67
    • 0024723058 scopus 로고
    • Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: Phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB
    • Fischer E., Günter K., Braun V. Involvement of ExbB and TonB in transport across the outer membrane of Escherichia coli: phenotypic complementation of exb mutants by overexpressed tonB and physical stabilization of TonB by ExbB. J. Bacteriol. 171:1989;5127-5134.
    • (1989) J. Bacteriol. , vol.171 , pp. 5127-5134
    • Fischer, E.1    Günter, K.2    Braun, V.3
  • 68
    • 0036330840 scopus 로고    scopus 로고
    • Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB
    • Dubuisson J.F., Vianney A., Lazzaroni J.C. Mutational analysis of the TolA C-terminal domain of Escherichia coli and genetic evidence for an interaction between TolA and TolB. J. Bacteriol. 184:2002;4620-4625.
    • (2002) J. Bacteriol. , vol.184 , pp. 4620-4625
    • Dubuisson, J.F.1    Vianney, A.2    Lazzaroni, J.C.3
  • 69
    • 0036182369 scopus 로고    scopus 로고
    • Salmonella enterica serovar typhimurium resistance to bile: Identification and characterization of the tolQRA cluster
    • Prouty A.M., Van Velkinburgh J.C., Gunn J.S. Salmonella enterica serovar typhimurium resistance to bile: identification and characterization of the tolQRA cluster. J. Bacteriol. 184:2002;1270-1276.
    • (2002) J. Bacteriol. , vol.184 , pp. 1270-1276
    • Prouty, A.M.1    Van Velkinburgh, J.C.2    Gunn, J.S.3
  • 70
    • 0036093944 scopus 로고    scopus 로고
    • The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB
    • Walburger A., Lazdunski C., Corda Y. The Tol/Pal system function requires an interaction between the C-terminal domain of TolA and the N-terminal domain of TolB. Mol. Microbiol. 44:2002;695-708.
    • (2002) Mol. Microbiol. , vol.44 , pp. 695-708
    • Walburger, A.1    Lazdunski, C.2    Corda, Y.3
  • 71
    • 0034970708 scopus 로고    scopus 로고
    • Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR
    • Germon P., Ray M.-C., Vianney A., Lazzaroni J.C. Energy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR. J. Bacteriol. 183:2001;4110-4114.
    • (2001) J. Bacteriol. , vol.183 , pp. 4110-4114
    • Germon, P.1    Ray, M.-C.2    Vianney, A.3    Lazzaroni, J.C.4
  • 72
    • 0029150033 scopus 로고
    • Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis
    • Sharp L.L., Zhou J.D., Blair D.F. Features of MotA proton channel structure revealed by tryptophan-scanning mutagenesis. Proc. Natl. Acad. Sci. U. S. A. 92:1995;7946-7956.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 7946-7956
    • Sharp, L.L.1    Zhou, J.D.2    Blair, D.F.3
  • 73
    • 0029083969 scopus 로고
    • Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli
    • Sharp L.L., Zhou J.D., Blair D.F. Tryptophan-scanning mutagenesis of MotB, an integral membrane protein essential for flagellar rotation in Escherichia coli. Biochemistry. 34:1995;9166-9171.
    • (1995) Biochemistry , vol.34 , pp. 9166-9171
    • Sharp, L.L.1    Zhou, J.D.2    Blair, D.F.3
  • 76
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J., Hasberli P., Smithies O. A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res. 12:1984;387-395.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Hasberli, P.2    Smithies, O.3
  • 77
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:1997;4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 78
    • 0000122573 scopus 로고
    • PHYLIP-phylogeny inference package (version 3.2)
    • Felsenstein J. PHYLIP-phylogeny inference package (version 3.2). Cladistics. 5:1989;164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 79
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng D.-F., Doolittle R.F. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 13:1990;375-387.
    • (1990) Methods Enzymol. , vol.13 , pp. 375-387
    • Feng, D.-F.1    Doolittle, R.F.2
  • 81
    • 0030902305 scopus 로고    scopus 로고
    • Three-dimensional model of sensory rhodopsin I reveals important restraints between the protein and the chromophore
    • Lin S.L., Yan B. Three-dimensional model of sensory rhodopsin I reveals important restraints between the protein and the chromophore. Protein Eng. 10:1997;197-206.
    • (1997) Protein Eng. , vol.10 , pp. 197-206
    • Lin, S.L.1    Yan, B.2
  • 82
    • 0035795114 scopus 로고    scopus 로고
    • Homologues of archaeal rhodopsins in plants, animals and fungi: Structural and functional predications for a putative fungal chaperone protein
    • Zhai Y., Heijne W.H.M., Smith D.W., Saier M.H. Jr. Homologues of archaeal rhodopsins in plants, animals and fungi: structural and functional predications for a putative fungal chaperone protein. Biochim. Biophys. Acta. 1511:2001;206-223.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 206-223
    • Zhai, Y.1    Heijne, W.H.M.2    Smith, D.W.3    Saier M.H., Jr.4
  • 83
    • 0024670659 scopus 로고
    • Dynamics of a tightly coupled mechanism for flagellar rotation. Bacterial motility, chemiosmotic coupling, proton motive force
    • Meister M., Caplan S.R., Berg H.C. Dynamics of a tightly coupled mechanism for flagellar rotation. Bacterial motility, chemiosmotic coupling, proton motive force. Biophys. J. 55:1989;905-914.
    • (1989) Biophys. J. , vol.55 , pp. 905-914
    • Meister, M.1    Caplan, S.R.2    Berg, H.C.3
  • 84
    • 0031975098 scopus 로고    scopus 로고
    • Role of the Haemophilus ducreyi Ton system in internalization of heme from hemoglobin
    • Elkins C., Totten P.A., Olsen B., Thomas C.E. Role of the Haemophilus ducreyi Ton system in internalization of heme from hemoglobin. Infect. Immun. 66:1998;151-160.
    • (1998) Infect. Immun. , vol.66 , pp. 151-160
    • Elkins, C.1    Totten, P.A.2    Olsen, B.3    Thomas, C.E.4
  • 85
    • 0025879664 scopus 로고
    • Mutant MotB proteins in Escherichia coli
    • Blair D.F., Kim D.Y., Berg H.C. Mutant MotB proteins in Escherichia coli. J. Bacteriol. 179:1991;4049-4055.
    • (1991) J. Bacteriol. , vol.179 , pp. 4049-4055
    • Blair, D.F.1    Kim, D.Y.2    Berg, H.C.3


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