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Volumn 15, Issue 4, 2005, Pages 394-400

TonB-dependent outer membrane transport: Going for Baroque?

Author keywords

[No Author keywords available]

Indexed keywords

CYANOCOBALAMIN; ORGANOMETALLIC COMPOUND; PROTEIN; PROTEIN TONB; SIDEROPHORE; TRACE ELEMENT; UNCLASSIFIED DRUG;

EID: 23044489264     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.07.001     Document Type: Review
Times cited : (114)

References (38)
  • 1
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • H. Nikaido Molecular basis of bacterial outer membrane permeability revisited Microbiol Mol Biol Rev 67 2003 593 656
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 2
    • 0023027071 scopus 로고
    • Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB
    • M.D. Lundrigan, and R.J. Kadner Nucleotide sequence of the gene for the ferrienterochelin receptor FepA in Escherichia coli. Homology among outer membrane receptors that interact with TonB J Biol Chem 261 1986 10797 10801
    • (1986) J Biol Chem , vol.261 , pp. 10797-10801
    • Lundrigan, M.D.1    Kadner, R.J.2
  • 3
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus pentapeptide among TonB-dependent colicins and receptors
    • E. Schramm, J. Mende, V. Braun, and R.M. Kamp Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonB-dependent colicins and receptors J Bacteriol 169 1987 3350 3357
    • (1987) J Bacteriol , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 4
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • A.D. Ferguson, E. Hofmann, J.W. Coulton, K. Diederichs, and W. Welte 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
  • 5
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • K.P. Locher, B. Rees, R. Koebnik, A. Mitschler, L. Moulinier, J.P. Rosenbusch, and D. Moras Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes Cell 95 1998 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
  • 8
    • 0042508859 scopus 로고    scopus 로고
    • Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
    • W.W. Yue, S. Grizot, and S.K. Buchanan Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA J Mol Biol 332 2003 353 368
    • (2003) J Mol Biol , vol.332 , pp. 353-368
    • Yue, W.W.1    Grizot, S.2    Buchanan, S.K.3
  • 9
    • 0242670022 scopus 로고    scopus 로고
    • Substrate induced transmembrane signalling in the cobalamin transporter BtuB
    • D.P. Chimento, A.K. Mohanty, R.J. Kadner, and M.C. Wiener Substrate induced transmembrane signalling 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
  • 10
    • 14144255323 scopus 로고    scopus 로고
    • The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6Å resolution
    • D. Cobessi, H. Celia, N. Folschweiller, I.J. Schalk, M.A. Abdallah, and F. Pattus The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6Å resolution J Mol Biol 347 2005 121 134
    • (2005) J Mol Biol , vol.347 , pp. 121-134
    • Cobessi, D.1    Celia, H.2    Folschweiller, N.3    Schalk, I.J.4    Abdallah, M.A.5    Pattus, F.6
  • 11
    • 0030925485 scopus 로고    scopus 로고
    • Surface signaling: Novel transcription initiation mechanism starting from the cell surface
    • V. Braun Surface signaling: novel transcription initiation mechanism starting from the cell surface Arch Microbiol 167 1997 325 331
    • (1997) Arch Microbiol , vol.167 , pp. 325-331
    • Braun, V.1
  • 12
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • H.J. Merianos, N. Cadieux, C.H. Lin, R.J. Kadner, and D.S. Cafiso Substrate-induced exposure of an energy-coupling motif of a membrane transporter Nat Struct Biol 7 2000 205 209
    • (2000) Nat Struct Biol , vol.7 , pp. 205-209
    • Merianos, H.J.1    Cadieux, N.2    Lin, C.H.3    Kadner, R.J.4    Cafiso, D.S.5
  • 13
    • 0036786885 scopus 로고    scopus 로고
    • Structure and dynamics of the beta-barrel of the membrane transporter BtuB by site-directed spin labeling
    • G.E. Fanucci, N. Cadieux, C.A. Piedmont, R.J. Kadner, and D.S. Cafiso Structure and dynamics of the beta-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
  • 14
    • 0242569215 scopus 로고    scopus 로고
    • Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein
    • G.E. Fanucci, and D.S. Cafiso Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein Biochemistry 42 2003 13106 13112
    • (2003) Biochemistry , vol.42 , pp. 13106-13112
    • Fanucci, G.E.1    Cafiso, D.S.2
  • 15
    • 0141703294 scopus 로고    scopus 로고
    • Differential substrate induced signalling through the Ton-B dependent transporter BtuB
    • N. Cadieux, P.G. Phan, D.S. Cafiso, and R.J. Kadner Differential substrate induced signalling through the Ton-B dependent transporter BtuB Proc Natl Acad Sci USA 100 2003 10688 10693
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10688-10693
    • Cadieux, N.1    Phan, P.G.2    Cafiso, D.S.3    Kadner, R.J.4
  • 16
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat Rev Mol Cell Biol 6 2005 197 208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 17
    • 0022931302 scopus 로고
    • Sequence-imposed structural constraints in the TonB protein of E. coli
    • J.S. Evans, B.A. Levine, I.P. Trayer, C.J. Dorman, and C.F. Higgins Sequence-imposed structural constraints in the TonB protein of E. coli FEBS Lett 208 1986 211 216
    • (1986) FEBS Lett , vol.208 , pp. 211-216
    • Evans, J.S.1    Levine, B.A.2    Trayer, I.P.3    Dorman, C.J.4    Higgins, C.F.5
  • 19
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • C. Chang, A. Mooser, A. Pluckthun, and A. Wlodawer Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold J Biol Chem 276 2001 27535 27540
    • (2001) J Biol Chem , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 20
    • 0041704803 scopus 로고    scopus 로고
    • Molecular modeling of the bacterial outer membrane receptor energizer, exbBD/TonB, based on homology with the flagellar motor, MotAB
    • Y.F. Zhai, W. Heijne, and M.H. Saier Jr. Molecular modeling of the bacterial outer membrane receptor energizer, exbBD/TonB, based on homology with the flagellar motor, MotAB Biochim Biophys Acta 1614 2003 201 210
    • (2003) Biochim Biophys Acta , vol.1614 , pp. 201-210
    • Zhai, Y.F.1    Heijne, W.2    Saier Jr., M.H.3
  • 23
    • 13244255594 scopus 로고    scopus 로고
    • Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments
    • J. Ködding, F. Killig, P. Polzer, S.P. Howard, K. Diederichs, and W. Welte Crystal structure of a 92-residue C-terminal fragment of TonB from Escherichia coli reveals significant conformational changes compared to structures of smaller TonB fragments J Biol Chem 280 2005 3022 3028 The crystal structure of a 92-residue C-terminal TonB construct is presented. The construct is monomeric in solution. Interestingly, the crystal structure is a dimer. However, the structures of the individual TonB monomers, as well as the dimer interface, are significantly different from those seen in the short C-terminal TonB construct structure [19]. Specifically, the dimer interface of the longer construct is a short domain-swapped β strand at the C terminus.
    • (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
  • 24
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the C-terminal domain of TonB and interactions studies with TonB box peptides
    • ••], except for the absence of the domain-swapped β strand. In addition, the binding of ten-residue peptides (corresponding to the Ton boxes of FhuA, FepA and BtuB) was characterized by isothermal titration calorimetry and chemical shift perturbations.
    • (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
  • 25
    • 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
    • N. Cadieux, and R.J. Kadner 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 1999 10673 10678
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 26
    • 0033764762 scopus 로고    scopus 로고
    • Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein
    • N. Cadieux, C. Bradbeer, and R.J. Kadner Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein J Bacteriol 182 2000 5954 5961
    • (2000) J Bacteriol , vol.182 , pp. 5954-5961
    • Cadieux, N.1    Bradbeer, C.2    Kadner, R.J.3
  • 27
    • 0346334403 scopus 로고    scopus 로고
    • Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction
    • J. Ghosh, and K. Postle Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction Mol Microbiol 51 2004 203 213
    • (2004) Mol Microbiol , vol.51 , pp. 203-213
    • Ghosh, J.1    Postle, K.2
  • 28
    • 12344263219 scopus 로고    scopus 로고
    • Disulfide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein
    • J. Ghosh, and K. Postle Disulfide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein Mol Microbiol 55 2005 276 288
    • (2005) Mol Microbiol , vol.55 , pp. 276-288
    • Ghosh, J.1    Postle, K.2
  • 29
    • 0141727626 scopus 로고    scopus 로고
    • In vivo evidence for TonB dimerization
    • A. Sauter, S.P. Howard, and V. Braun In vivo evidence for TonB dimerization J Bacteriol 185 2003 5747 5754
    • (2003) J Bacteriol , vol.185 , pp. 5747-5754
    • Sauter, A.1    Howard, S.P.2    Braun, V.3
  • 30
    • 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
    • C.M. Khursigara, G. De Crescenzo, P.D. Pawelek, and J.W. Coulton 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 2005 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
  • 31
    • 14644388782 scopus 로고    scopus 로고
    • Kinetic analyses reveal multiple steps in forming TonB-FhuA complexes from Escherichia coli
    • C.M. Khursigara, G. De Crescenzo, P.D. Pawelek, and J.W. Coulton Kinetic analyses reveal multiple steps in forming TonB-FhuA complexes from Escherichia coli Biochemistry 44 2005 3441 3453
    • (2005) Biochemistry , vol.44 , pp. 3441-3453
    • Khursigara, C.M.1    De Crescenzo, G.2    Pawelek, P.D.3    Coulton, J.W.4
  • 32
    • 0035845572 scopus 로고    scopus 로고
    • The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, bins its siderophore in the absence of the transmembrane barrel domain
    • K.C. Usher, E. Özkan, K.H. Gardner, and J. Deisenhofer The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, bins its siderophore in the absence of the transmembrane barrel domain Proc Natl Acad Sci USA 98 2001 10676 10681
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10676-10681
    • Usher, K.C.1    Özkan, E.2    Gardner, K.H.3    Deisenhofer, J.4
  • 33
    • 1942532328 scopus 로고    scopus 로고
    • The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane β-barrel
    • M. Oke, R. Sarra, R. Ghirlando, S. Farnaud, A.R. Gorringe, R.W. Evans, and S.K. Buchanan The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane β-barrel FEBS Lett 564 2004 294 300
    • (2004) FEBS Lett , vol.564 , pp. 294-300
    • Oke, M.1    Sarra, R.2    Ghirlando, R.3    Farnaud, S.4    Gorringe, A.R.5    Evans, R.W.6    Buchanan, S.K.7
  • 34
    • 0037671392 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A comparative study of the ferrichrome-free and bound states
    • J.D. Faraldo-Gomez, G.R. Smith, and M.S.P. Sansom Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states Biophys J 85 2003 1406 1420
    • (2003) Biophys J , vol.85 , pp. 1406-1420
    • Faraldo-Gomez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 35
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • D.P. Chimento, R.J. Kadner, and M.C. Wiener Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle Proteins 59 2005 240 251 This paper presents a detailed structural comparison and analysis of the four TBDT structures (FhuA, FepA, FecA and BtuB) available at that time (FpvA has since been determined [10]). The results of this paper include: identification of highly conserved structural motifs in TBDTs, hypotheses about the possible mechanistic roles of these conserved motifs and analysis of the hatch-barrel interfaces in TBDT structures. This interface analysis suggests that the hatch domains are extensively hydrated within the β barrel by water molecules with excess hydrogen-bonding capacity. The implication of this result is that this 'water bushing' reduces the energetic barrier of perturbing the hatch-barrel interface during the transport cycle. That is to say, substantial conformational change or partial/full removal of the hatch from the barrel during the transport cycle is not prohibited by properties of the hatch-barrel interface. Lastly, similarities between the hatch domains (four-stranded β-sheet core) and proteins used in single-molecule unfolding studies are noted, with the hypothesis that only very modest force exerted by TonB upon the hatch domain may suffice to cause substantial conformational change or unfolding.
    • (2005) Proteins , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 36
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • T.E. Letain, and K. Postle 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, K.2
  • 37
    • 0038385104 scopus 로고    scopus 로고
    • In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
    • R.A. Larsen, and K. Postle In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli J Bacteriol 49 2003 211 218
    • (2003) J Bacteriol , vol.49 , pp. 211-218
    • Larsen, R.A.1    Postle, K.2
  • 38
    • 0027484363 scopus 로고
    • Identification of a residue in the translocation pathway of a membrane carrier
    • R.T. Yan, and P.C. Maloney Identification of a residue in the translocation pathway of a membrane carrier Cell 75 1993 37 44
    • (1993) Cell , vol.75 , pp. 37-44
    • Yan, R.T.1    Maloney, P.C.2


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