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Volumn 20, Issue 3-4, 2007, Pages 453-465

TonB-dependent energy transduction between outer and cytoplasmic membranes

Author keywords

B group colicins; Crystal and NMR structures; Iron transport; Outer membrane; TonB

Indexed keywords

BACTERIAL PROTEIN; IRON; PROTEIN TONB; PROTON; UNCLASSIFIED DRUG;

EID: 34248647893     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-006-9071-6     Document Type: Conference Paper
Times cited : (141)

References (70)
  • 1
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates direct interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell PE, Nau CD, Brown JT, Konisky J, Kadner RJ (1990) Genetic suppression demonstrates direct interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J Bacteriol 172:3826-3829
    • (1990) J Bacteriol , vol.172 , pp. 3826-3829
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, R.J.5
  • 2
    • 0037715359 scopus 로고    scopus 로고
    • Flagellar movement driven by proton translocation
    • Blair DF (2003) Flagellar movement driven by proton translocation. FEBS Lett 545:86-95
    • (2003) FEBS Lett , vol.545 , pp. 86-95
    • Blair, D.F.1
  • 3
    • 0024452245 scopus 로고
    • The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity
    • Braun V (1989) The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity. J Bacteriol 171:6387-6390
    • (1989) J Bacteriol , vol.171 , pp. 6387-6390
    • Braun, V.1
  • 4
    • 0027193060 scopus 로고
    • Evolutionary relationship of uptake systems for biopolymers in Escherichia coli: Cross-complementation between the TonB-ExbB-ExbD and the TolA-TolQ-TolR proteins
    • Braun V, Herrmann C (1993) Evolutionary relationship of uptake systems for biopolymers in Escherichia coli: cross-complementation between the TonB-ExbB-ExbD and the TolA-TolQ-TolR proteins. Mol Microbiol 8:261-268
    • (1993) Mol Microbiol , vol.8 , pp. 261-268
    • Braun, V.1    Herrmann, C.2
  • 5
    • 3042615583 scopus 로고    scopus 로고
    • Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12
    • Braun V, Herrmann C (2004) Point mutations in transmembrane helices 2 and 3 of ExbB and TolQ affect their activities in Escherichia coli K-12. J Bacteriol 186:4402-4406
    • (2004) J Bacteriol , vol.186 , pp. 4402-4406
    • Braun, V.1    Herrmann, C.2
  • 6
    • 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, Killman H, Traub I (1996) 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 178:2836-2845
    • (1996) J Bacteriol , vol.178 , pp. 2836-2845
    • Braun, V.1    Gaisser, S.2    Herrmann, C.3    Kampfenkel, K.4    Killman, H.5    Traub, I.6
  • 7
    • 0036589164 scopus 로고    scopus 로고
    • Ton-dependent colicins and microcins: Modular design and evolution
    • Braun V, Patzer SI, Hantke K (2002) Ton-dependent colicins and microcins: modular design and evolution. Biochimie 84:365-380
    • (2002) Biochimie , vol.84 , pp. 365-380
    • Braun, V.1    Patzer, S.I.2    Hantke, K.3
  • 9
    • 0032849375 scopus 로고    scopus 로고
    • Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
    • Cadieux N, Kadner RJ (1999) Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter. Proc Natl Acad Sci USA 96:10673-10678
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 11
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • Cascales E, Lloubes R, Sturgis JN (2001) The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Mol Microbiol 42:795-807
    • (2001) Mol Microbiol , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 12
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric carboxy-terminal domain of TonB reveals a novel fold
    • Chang C, Mooser A, Plückthun A, Wiodawer A (2001) Crystal structure of the dimeric carboxy-terminal domain of TonB reveals a novel fold. J Biol Chem 276:27535-27540
    • (2001) J Biol Chem , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Plückthun, A.3    Wiodawer, A.4
  • 13
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • Chimento DP, Kadner RJ, Weiner MC (2005) Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins 59:240-251
    • (2005) Proteins , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Weiner, M.C.3
  • 15
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson AD, Hofmann E, Coulton JW, Diederiche K, Welte W (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282:2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederiche, K.4    Welte, W.5
  • 17
    • 0034970708 scopus 로고    scopus 로고
    • Energy-dependent conformational change in the TolA protein of Escherichia coli involves its amino-terminal domain, TolQ, and TolR
    • Germon P, Ray MC, Vianney A, Lazzaroni J-C (2001) Energy-dependent conformational change in the TolA protein of Escherichia coli involves its amino-terminal domain, TolQ, and TolR. J Bacteriol 183:4110-4114
    • (2001) J Bacteriol , vol.183 , pp. 4110-4114
    • Germon, P.1    Ray, M.C.2    Vianney, A.3    Lazzaroni, J.-C.4
  • 18
    • 0346334403 scopus 로고    scopus 로고
    • Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction
    • Ghosh J, Postle K (2004) Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction. Mol Microbiol 51:203-213
    • (2004) Mol Microbiol , vol.51 , pp. 203-213
    • Ghosh, J.1    Postle, K.2
  • 19
    • 12344263219 scopus 로고    scopus 로고
    • Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein
    • Ghosh J, Postle K (2005) Disulphide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein. Mol Microbiol 55:276-288
    • (2005) Mol Microbiol , vol.55 , pp. 276-288
    • Ghosh, J.1    Postle, K.2
  • 20
    • 0024368556 scopus 로고
    • Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport
    • Gudmundsdottir A, Bell PE, Lundrigan MD, Bradbeer C, Kadner RJ (1989) Point mutations in a conserved region (TonB box) of Escherichia coli outer membrane protein BtuB affect vitamin B12 transport. J Bacteriol 171:6526-6533
    • (1989) J Bacteriol , vol.171 , pp. 6526-6533
    • Gudmundsdottir, A.1    Bell, P.E.2    Lundrigan, M.D.3    Bradbeer, C.4    Kadner, R.J.5
  • 22
    • 0036723874 scopus 로고    scopus 로고
    • ExbB and ExbD do not function independently in TonB-dependent energy transduction
    • Held KG, Postle K (2002) ExbB and ExbD do not function independently in TonB-dependent energy transduction. J Bacteriol 184:5170-5173
    • (2002) J Bacteriol , vol.184 , pp. 5170-5173
    • Held, K.G.1    Postle, K.2
  • 23
    • 0021950967 scopus 로고
    • 12 receptor protein in the outer membrane of Escherichia coli
    • 12 receptor protein in the outer membrane of Escherichia coli. J Bacteriol 161:904-908
    • (1985) J Bacteriol , vol.161 , pp. 904-908
    • Heller, K.1    Kadner, R.J.2
  • 24
    • 0023886391 scopus 로고
    • Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli
    • Heller K, Kadner RJ, Günter K (1988) Suppression of the btuB451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli. Gene 64:147-153
    • (1988) Gene , vol.64 , pp. 147-153
    • Heller, K.1    Kadner, R.J.2    Günter, K.3
  • 25
    • 0033563413 scopus 로고    scopus 로고
    • Two strategies for sequence comparison: Profile-preprocessed and secondary structure-induced multiple alignment
    • Heringa J (1999) Two strategies for sequence comparison: profile-preprocessed and secondary structure-induced multiple alignment. Computers Chem 23:341-364
    • (1999) Computers Chem , vol.23 , pp. 341-364
    • Heringa, J.1
  • 26
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs PI, Myers PS, Postle K (1998) Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers. J Bacteriol 180:6031-6038
    • (1998) J Bacteriol , vol.180 , pp. 6031-6038
    • Higgs, P.I.1    Myers, P.S.2    Postle, K.3
  • 27
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA
    • Higgs PI, Larsen RA, Postle K (2002a) Quantification of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA. Mol Microbiol 44:271-281
    • (2002) Mol Microbiol , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 28
    • 0034805380 scopus 로고    scopus 로고
    • In vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli
    • Howard SP, Herrmann C, Stratilo CW, Braun V (2001) In vivo synthesis of the periplasmic domain of TonB inhibits transport through the FecA and FhuA iron siderophore transporters of Escherichia coli. J Bacteriol 183:5885-5895
    • (2001) J Bacteriol , vol.183 , pp. 5885-5895
    • Howard, S.P.1    Herrmann, C.2    Stratilo, C.W.3    Braun, V.4
  • 29
    • 0028280919 scopus 로고
    • Role of the TonB amino terminus in energy transduction between membranes
    • Jaskula JC, Letain TE, Roof SK, Skare JT, Postle K (1994) Role of the TonB amino terminus in energy transduction between membranes. J Bacteriol 176:2326-2338
    • (1994) J Bacteriol , vol.176 , pp. 2326-2338
    • Jaskula, J.C.1    Letain, T.E.2    Roof, S.K.3    Skare, J.T.4    Postle, K.5
  • 30
    • 0027154838 scopus 로고
    • A sequence-specific function for the amino-terminal signal-like sequence of the TonB protein
    • Karlsson M, Hannavy K, Higgins CF (1993) A sequence-specific function for the amino-terminal signal-like sequence of the TonB protein. Mol Microbiol 8:379-388
    • (1993) Mol Microbiol , vol.8 , pp. 379-388
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 31
    • 0027165444 scopus 로고
    • The molecular interaction between components of the TonB-ExbBD-dependent and of the TolQRA-dependent bacterial uptake systems
    • Koebnik R (1993) The molecular interaction between components of the TonB-ExbBD-dependent and of the TolQRA-dependent bacterial uptake systems. Mol Microbiol 9:219
    • (1993) Mol Microbiol , vol.9 , pp. 219
    • Koebnik, R.1
  • 32
    • 1642287423 scopus 로고    scopus 로고
    • Dimerization of TonB is not essential for tis binding to the outer membrane siderophore receptor FhuA of Escherichia coli
    • Ködding J, Howard SP, Kaufmann L, Potzer P, Lustig A, Welte W (2004) Dimerization of TonB is not essential for tis binding to the outer membrane siderophore receptor FhuA of Escherichia coli. J Biol Chem 279:9978-9986
    • (2004) J Biol Chem , vol.279 , pp. 9978-9986
    • Ködding, J.1    Howard, S.P.2    Kaufmann, L.3    Potzer, P.4    Lustig, A.5    Welte, W.6
  • 33
    • 13244255594 scopus 로고    scopus 로고
    • Crystal structure of a 92-residue carboxy-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments
    • Ködding J, Killig F, Polzer P, Howard SP, Diederichs K, Welte W (2005) Crystal structure of a 92-residue carboxy-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments. J Biol Chem 280:3022-3028
    • (2005) J Biol Chem , vol.280 , pp. 3022-3028
    • Ködding, J.1    Killig, F.2    Polzer, P.3    Howard, S.P.4    Diederichs, K.5    Welte, W.6
  • 34
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima S, Blair DF (2001) Conformational change in the stator of the bacterial flagellar motor. Biochemistry 40:13041-13050
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2
  • 35
    • 1542320184 scopus 로고    scopus 로고
    • Enhanced binding of TonB to a ligand-loaded outer membrane receptor. Role of the oligomeric state of TonB in formation of a functional FhuA-TonB complex
    • Khursigara CM, De Crescenzo G, Pawelek PD, Coulton JW (2004) Enhanced binding of TonB to a ligand-loaded outer membrane receptor. Role of the oligomeric state of TonB in formation of a functional FhuA-TonB complex. J Biol Chem 279:7405-7412
    • (2004) J Biol Chem , vol.279 , pp. 7405-7412
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 36
    • 17744372268 scopus 로고    scopus 로고
    • Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli
    • Khursigara CM, De Crescenzo G, Pawelek PD, Coulton JW (2005b) Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli. Protein Sci 14:1266-1273
    • (2005) Protein Sci , vol.14 , pp. 1266-1273
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 37
    • 0035896546 scopus 로고    scopus 로고
    • Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force
    • Larsen RA, Postle K (2001) Conserved residues Ser(16) and His(20) and their relative positioning are essential for TonB activity, cross-linking of TonB with ExbB, and the ability of TonB to respond to proton motive force. J Biol Chem 276:8111-8117
    • (2001) J Biol Chem , vol.276 , pp. 8111-8117
    • Larsen, R.A.1    Postle, K.2
  • 38
    • 0027730652 scopus 로고
    • The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein
    • Larsen RA, Wood GE, Postle K (1993) The conserved proline-rich motif is not essential for energy transduction by Escherichia coli TonB protein. Mol Microbiol 10:943-953
    • (1993) Mol Microbiol , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, G.E.2    Postle, K.3
  • 39
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (δV17) by a missense mutation in ExbB
    • Larsen RA, Thomas MT, Wood GE, Postle K (1994) Partial suppression of an Escherichia coli TonB transmembrane domain mutation (δV17) by a missense mutation in ExbB. Mol Microbiol 13:627-640
    • (1994) Mol Microbiol , vol.13 , pp. 627-640
    • Larsen, R.A.1    Thomas, M.T.2    Wood, G.E.3    Postle, K.4
  • 40
    • 0030911410 scopus 로고    scopus 로고
    • Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions
    • Larsen RA, Foster-Hartnett D, McIntosh MA, Postle K (1997) Regions of Escherichia coli TonB and FepA proteins essential for in vivo physical interactions. J Bacteriol 179:3213-3221
    • (1997) J Bacteriol , vol.179 , pp. 3213-3221
    • Larsen, R.A.1    Foster-Hartnett, D.2    McIntosh, M.A.3    Postle, K.4
  • 41
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen RA, Thomas MG, Postle K (1999) Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB. Mol Microbiol 31:1809-1824
    • (1999) Mol Microbiol , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 42
    • 0038385104 scopus 로고    scopus 로고
    • In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
    • Larsen RA, Letain TE, Postle K (2003) In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli. Mol Microbiol 49:211-218
    • (2003) Mol Microbiol , vol.49 , pp. 211-218
    • Larsen, R.A.1    Letain, T.E.2    Postle, K.3
  • 43
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Gram-negative bacteria
    • Letain TE, Postle K (1997) TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Gram-negative bacteria. Mol Microbiol 24:271-283
    • (1997) Mol Microbiol , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 44
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • Locher KP, Rees B, Koebnik R, Mitschler A, Moulinier l, Rosenbusch JP, Moras D (1998) Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell 95:771-778
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 45
    • 0000046526 scopus 로고    scopus 로고
    • Filamentous phage infection: Crystal structure of g3p in complex with its coreceptor, the carboxy-terminal domain of TolA
    • Lubkowski J, Hennecke F, Plückthun A, Wlodawer A (1999) Filamentous phage infection: crystal structure of g3p in complex with its coreceptor, the carboxy-terminal domain of TolA. Structure 7:711-722
    • (1999) Structure , vol.7 , pp. 711-722
    • Lubkowski, J.1    Hennecke, F.2    Plückthun, A.3    Wlodawer, A.4
  • 46
    • 0022577734 scopus 로고
    • Reduced activity of TonB-dependent functions in strains of Escherichia coli
    • Mann BJ, Holroyd CD, Bradbeer C, Kadner RJ (1986) Reduced activity of TonB-dependent functions in strains of Escherichia coli. FEMS Lett 33:255-260
    • (1986) FEMS Lett , vol.33 , pp. 255-260
    • Mann, B.J.1    Holroyd, C.D.2    Bradbeer, C.3    Kadner, R.J.4
  • 47
    • 0037312519 scopus 로고    scopus 로고
    • Analysis of residues determining specificity of Vibrio cholerae TonB1 for its receptors
    • Mey AR, Payne SM (2003) Analysis of residues determining specificity of Vibrio cholerae TonB1 for its receptors. J Bacteriol 185:1195-1207
    • (2003) J Bacteriol , vol.185 , pp. 1195-1207
    • Mey, A.R.1    Payne, S.M.2
  • 48
    • 28844503096 scopus 로고    scopus 로고
    • ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus
    • Neugebauer H, Herrmann C, Kammer W, Schwarz G, Nordheim A, Braun V (2005) ExbBD-dependent transport of maltodextrins through the novel MalA protein across the outer membrane of Caulobacter crescentus. J Bacteriol 187: 8300-8311
    • (2005) J Bacteriol , vol.187 , pp. 8300-8311
    • Neugebauer, H.1    Herrmann, C.2    Kammer, W.3    Schwarz, G.4    Nordheim, A.5    Braun, V.6
  • 50
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the carboxy-terminal domain of TonB and interaction studies with TonB box peptides
    • Peacock RS, Weljie AM, Howard SP, Price FD, Vogel HJ (2005) The solution structure of the carboxy-terminal domain of TonB and interaction studies with TonB box peptides. J Mol Biol 345:1185-1197
    • (2005) J Mol Biol , vol.345 , pp. 1185-1197
    • Peacock, R.S.1    Weljie, A.M.2    Howard, S.P.3    Price, F.D.4    Vogel, H.J.5
  • 52
    • 0020825487 scopus 로고
    • DNA sequence of the Escherichia coli tonB gene
    • Postle K, Good RF (1983) DNA sequence of the Escherichia coli tonB gene. Proc Natl Acad Sci USA 80:5235-5239
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 5235-5239
    • Postle, K.1    Good, R.F.2
  • 53
    • 0023715782 scopus 로고
    • Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus
    • Postle K, Skare JT (1988) Escherichia coli TonB protein is exported from the cytoplasm without proteolytic cleavage of its amino terminus. J Biol Chem 263:11000-11007
    • (1988) J Biol Chem , vol.263 , pp. 11000-11007
    • Postle, K.1    Skare, J.T.2
  • 54
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle K, Kadner RJ (2003) Touch and go: tying TonB to transport. Mol Microbiol 49:869-882
    • (2003) Mol Microbiol , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 56
    • 0024022151 scopus 로고
    • Genetics of the iron dicitrate transport system of Escherichia coli
    • Pressler U, Staudenmaier H, Zimmermann L, Braun V (1988) Genetics of the iron dicitrate transport system of Escherichia coli. J Bacteriol 170:2716-2724
    • (1988) J Bacteriol , vol.170 , pp. 2716-2724
    • Pressler, U.1    Staudenmaier, H.2    Zimmermann, L.3    Braun, V.4
  • 57
    • 0025992835 scopus 로고
    • Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions
    • Roof SK, Allard JD, Bertrand KP, Postle K (1991) Analysis of Escherichia coli TonB membrane topology by use of PhoA fusions. J Bacteriol 173:5554-5557
    • (1991) J Bacteriol , vol.173 , pp. 5554-5557
    • Roof, S.K.1    Allard, J.D.2    Bertrand, K.P.3    Postle, K.4
  • 58
    • 0343603660 scopus 로고    scopus 로고
    • A functional/phylogenetic classification system for transmembrane solute transporters
    • Saier MH Jr (2000) A functional/phylogenetic classification system for transmembrane solute transporters. Microbiol Mol Biol Rev 64:351-411
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 351-411
    • Saier Jr., M.H.1
  • 59
    • 0141727626 scopus 로고    scopus 로고
    • In vivo evidence for TonB dimerization
    • Sauter A, Howard SP, Braun V (2003) In vivo evidence for TonB dimerization. J Bacteriol 185:5747-5754
    • (2003) J Bacteriol , vol.185 , pp. 5747-5754
    • Sauter, A.1    Howard, S.P.2    Braun, V.3
  • 60
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • Schöffler H, Braun V (1989) Transport across the outer membrane of Escherichia coli via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol Gen Genet 217:378-383
    • (1989) Mol Gen Genet , vol.217 , pp. 378-383
    • Schöffler, H.1    Braun, V.2
  • 61
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • Schramm E, Mende J, Braun V, Kamp RM (1987) Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors. J Bacteriol 169:3350-3357
    • (1987) J Bacteriol , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 62
    • 0035136784 scopus 로고    scopus 로고
    • The two TonB systems of Vibrio cholerae: Redundant and specific functions
    • Seliger S, Mey A, Valle A, Payne S (2001) The two TonB systems of Vibrio cholerae: redundant and specific functions. Mol Microbiol 39:801-812
    • (2001) Mol Microbiol , vol.39 , pp. 801-812
    • Seliger, S.1    Mey, A.2    Valle, A.3    Payne, S.4
  • 63
    • 33744780736 scopus 로고    scopus 로고
    • Outer membrane active transport: Structure of the BtuB:TonB complex
    • Shultis DD, Purdy MD, Banchs CN, Wiener MC (2006) Outer membrane active transport: structure of the BtuB:TonB complex. Science 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
  • 65
    • 0024413265 scopus 로고
    • A mutation in the amino terminus of a hybrid TrpC-TonB protein relieves overproduction lethality and results in cytoplasmic accumulation
    • Skare JT, Roof SK, Postle K (1989) A mutation in the amino terminus of a hybrid TrpC-TonB protein relieves overproduction lethality and results in cytoplasmic accumulation. J Bacteriol 171:4442-4447
    • (1989) J Bacteriol , vol.171 , pp. 4442-4447
    • Skare, J.T.1    Roof, S.K.2    Postle, K.3
  • 66
    • 0027168466 scopus 로고
    • Activity domains of the TonB protein
    • Traub I, Gaisser S, Braun V (1993) Activity domains of the TonB protein. Mol Microbiol 8:409-423
    • (1993) Mol Microbiol , vol.8 , pp. 409-423
    • Traub, I.1    Gaisser, S.2    Braun, V.3
  • 67
    • 0026533769 scopus 로고
    • In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide
    • Tuckman M, Osburne MS (1992) In vivo inhibition of TonB-dependent processes by a TonB box consensus pentapeptide. J Bacteriol 174:320-323
    • (1992) J Bacteriol , vol.174 , pp. 320-323
    • Tuckman, M.1    Osburne, M.S.2
  • 68
    • 23044489264 scopus 로고    scopus 로고
    • TonB-dependent outer membrane transport: Going for Baroque?
    • Weiner MC (2005) TonB-dependent outer membrane transport: going for Baroque? Curr Opin Struct Biol 15: 394-400
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 394-400
    • Weiner, M.C.1
  • 69
    • 0037102135 scopus 로고    scopus 로고
    • Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: Evidence for an evolutionary relationship with the TonB transporter protein
    • Witty M, Sanz C, Shah A, Grossmann JG, Mizuguchi K, Perham RN, Luisi B (2002) Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein. EMBO J 21:4207-4218
    • (2002) EMBO J , vol.21 , pp. 4207-4218
    • Witty, M.1    Sanz, C.2    Shah, A.3    Grossmann, J.G.4    Mizuguchi, K.5    Perham, R.N.6    Luisi, B.7
  • 70
    • 0041704803 scopus 로고    scopus 로고
    • Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB
    • Zhai YF, Heijne W, Saier MH Jr (2003) Molecular modeling of the bacterial outer membrane receptor energizer, ExbBD/TonB, based on homology with the flagellar motor, MotAB. Biochim Biophys Acta 1614:201-210
    • (2003) Biochim Biophys Acta , vol.1614 , pp. 201-210
    • Zhai, Y.F.1    Heijne, W.2    Saier Jr., M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.