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S.K. Buchanan, B.S. Smith, L. Venkatramani, D. Xia, L. Esser, M. Palnitkar, R. Chakraborty, D. van der Helm, and J. Deisenhofer Crystal structure of the outer membrane active transporter FepA from Escherichia coli Nat Struct Biol 6 1999 56 63
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Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
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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
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Substrate induced transmembrane signalling in the cobalamin transporter BtuB
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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
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The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6Å resolution
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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
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Substrate-induced exposure of an energy-coupling motif of a membrane transporter
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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
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Structure and dynamics of the beta-barrel of the membrane transporter BtuB by site-directed spin labeling
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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
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Spectroscopic evidence that osmolytes used in crystallization buffers inhibit a conformation change in a membrane protein
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Differential substrate induced signalling through the Ton-B dependent transporter BtuB
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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
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Intrinsically unstructured proteins and their functions
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H.J. Dyson, and P.E. Wright Intrinsically unstructured proteins and their functions Nat Rev Mol Cell Biol 6 2005 197 208
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Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli
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S. Brewer, M. Tolley, I.P. Trayer, G.C. Barr, C.J. Dorman, K. Hannavy, C.F. Higgins, J.S. Evans, B.A. Levine, and M.R. Wormald Structure and function of X-Pro dipeptide repeats in the TonB proteins of Salmonella typhimurium and Escherichia coli J Mol Biol 216 1990 883 895
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Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
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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
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0041704803
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Molecular modeling of the bacterial outer membrane receptor energizer, exbBD/TonB, based on homology with the flagellar motor, MotAB
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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
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Zhai, Y.F.1
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13244255594
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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
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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.
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Ködding, J.1
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24
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11844269327
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The solution structure of the C-terminal domain of TonB and interactions studies with TonB box peptides
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••], 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.
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25
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0032849375
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Site-directed disulfide bonding reveals an interaction site between energy-coupling protein TonB and BtuB, the outer membrane cobalamin transporter
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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
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Cadieux, N.1
Kadner, R.J.2
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0033764762
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Sequence changes in the ton box region of BtuB affect its transport activities and interaction with TonB protein
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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
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0346334403
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Evidence for dynamic clustering of carboxy-terminal aromatic amino acids in TonB-dependent energy transduction
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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
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Postle, K.2
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12344263219
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Disulfide trapping of an in vivo energy-dependent conformation of Escherichia coli TonB protein
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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
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Postle, K.2
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0141727626
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In vivo evidence for TonB dimerization
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A. Sauter, S.P. Howard, and V. Braun In vivo evidence for TonB dimerization J Bacteriol 185 2003 5747 5754
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Sauter, A.1
Howard, S.P.2
Braun, V.3
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30
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17744372268
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Deletion of the proline-rich region of TonB disrupts formation of a 2:1 complex with FhuA, an outer membrane receptor of Escherichia coli
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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
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Khursigara, C.M.1
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31
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14644388782
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Kinetic analyses reveal multiple steps in forming TonB-FhuA complexes from Escherichia coli
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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
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Biochemistry
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Khursigara, C.M.1
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32
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0035845572
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The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, bins its siderophore in the absence of the transmembrane barrel domain
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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
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Usher, K.C.1
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Gardner, K.H.3
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33
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1942532328
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The plug domain of a neisserial TonB-dependent transporter retains structural integrity in the absence of its transmembrane β-barrel
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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
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Oke, M.1
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0037671392
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Molecular dynamics simulations of the bacterial outer membrane protein FhuA: A comparative study of the ferrichrome-free and bound states
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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
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16344373729
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Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
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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.
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Proteins
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Chimento, D.P.1
Kadner, R.J.2
Wiener, M.C.3
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36
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0030943591
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TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
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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
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Letain, T.E.1
Postle, K.2
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0038385104
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In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
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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
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J Bacteriol
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Larsen, R.A.1
Postle, K.2
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0027484363
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Identification of a residue in the translocation pathway of a membrane carrier
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R.T. Yan, and P.C. Maloney Identification of a residue in the translocation pathway of a membrane carrier Cell 75 1993 37 44
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