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Journal of Bacteriology
Volumn 197, Issue 11, 2015, Pages 1873-1885
Membrane protein complex ExbB4-ExbD1-TonB1 from Escherichia coli demonstrates conformational plasticity
Author keywords

[No Author keywords available]
Indexed keywords

IRON; MEMBRANE PROTEIN; PROTEIN EXBB4; PROTEIN EXBD1; PROTEIN TONB1; UNCLASSIFIED DRUG; ESCHERICHIA COLI PROTEIN; EXBB PROTEIN, E COLI; EXBD PROTEIN, E COLI; PROTEIN BINDING; TONB PROTEIN, E COLI;
EID: 84929439298     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00069-15     Document Type: Article
Times cited : (20)
References (93)
  • 1
    • 84863899006 scopus 로고    scopus 로고
    • Nutritional immunity: transition metals at the pathogen-host interface
    • Hood MI, Skaar EP. 2012. Nutritional immunity: transition metals at the pathogen-host interface. Nat Rev Microbiol 10:525-537. http://dx.doi.org/10.1038/nrmicro2836.
    • (2012) Nat Rev Microbiol , vol.10 , pp. 525-537
    • Hood, M.I.1    Skaar, E.P.2
  • 2
    • 84897921620 scopus 로고    scopus 로고
    • Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence
    • Porcheron G, Garénaux A, Proulx J, Sabri M, Dozois CM. 2013. Iron, copper, zinc, and manganese transport and regulation in pathogenic Enterobacteria: correlations between strains, site of infection and the relative importance of the different metal transport systems for virulence. Front Cell Infect Microbiol 3:90. http://dx.doi.org/10.3389/fcimb.2013.00090.
    • (2013) Front Cell Infect Microbiol , vol.3 , pp. 90
    • Porcheron, G.1    Garénaux, A.2    Proulx, J.3    Sabri, M.4    Dozois, C.M.5
  • 3
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: transcriptional metalloregulation by the Fur protein
    • Escolar L, Pérez-Martín J, de Lorenzo V. 1999. Opening the iron box: transcriptional metalloregulation by the Fur protein. J Bacteriol 181: 6223-6229.
    • (1999) J Bacteriol , vol.181 , pp. 6223-6229
    • Escolar, L.1    Pérez-Martín, J.2    de Lorenzo, V.3
  • 4
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke K. 2001. Iron and metal regulation in bacteria. Curr Opin Microbiol 4:172-177. http://dx.doi.org/10.1016/S1369-5274(00)00184-3.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 172-177
    • Hantke, K.1
  • 5
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. 2003. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 67:593-656. http://dx.doi.org/10.1128/MMBR.67.4.593-656.2003.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 6
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson AD, Hofmann E, Coulton JW, Diederichs K, Welte W. 1998. Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282:2215-2220. http://dx.doi.org/10.1126/science.282.5397.2215.
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 7
    • 77956505672 scopus 로고    scopus 로고
    • TonBdependent transporters: regulation, structure, and function
    • Noinaj N, Guillier M, Barnard Travis J, Buchanan SK. 2010. TonBdependent transporters: regulation, structure, and function. Annu Rev Microbiol 64:43-60. http://dx.doi.org/10.1146/annurev.micro.112408.134247.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 43-60
    • Noinaj, N.1    Guillier, M.2    Barnard Travis, J.3    Buchanan, S.K.4
  • 8
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonBdependent colicins and receptors
    • Schramm E, Mende J, Braun V, Kamp RM. 1987. Nucleotide sequence of the colicin B activity gene cba: consensus pentapeptide among TonBdependent 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
  • 9
    • 78651364685 scopus 로고    scopus 로고
    • TonB or not TonB: is that the question?
    • Krewulak KD, Vogel HJ. 2011. TonB or not TonB: is that the question? Biochem Cell Biol 89:87-97. http://dx.doi.org/10.1139/O10-141.
    • (2011) Biochem Cell Biol , vol.89 , pp. 87-97
    • Krewulak, K.D.1    Vogel, H.J.2
  • 10
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle
    • Chimento DP, Kadner RJ, Wiener MC. 2005. Comparative structural analysis of TonB-dependent outer membrane transporters: implications for the transport cycle. Proteins 59:240-251. http://dx.doi.org/10.1002/prot.20416.
    • (2005) Proteins , vol.59 , pp. 240-251
    • Chimento, D.P.1    Kadner, R.J.2    Wiener, M.C.3
  • 11
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • Merianos HJ, Cadieux N, Lin CH, Kadner RJ, Cafiso DS. 2000. Substrate-induced exposure of an energy-coupling motif of a membrane transporter. Nat Struct Biol 7:205-209. http://dx.doi.org/10.1038/73309.
    • (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
  • 12
    • 0037452539 scopus 로고    scopus 로고
    • Substrate-induced conformational changes of the periplasmic Nterminus of an outer-membrane transporter by site-directed spin labeling
    • Fanucci GE, Coggshall KA, Cadieux N, Kim M, Kadner RJ, Cafiso DS. 2003. Substrate-induced conformational changes of the periplasmic Nterminus of an outer-membrane transporter by site-directed spin labeling. Biochemistry 42:1391-1400. http://dx.doi.org/10.1021/bi027120z.
    • (2003) Biochemistry , vol.42 , pp. 1391-1400
    • Fanucci, G.E.1    Coggshall, K.A.2    Cadieux, N.3    Kim, M.4    Kadner, R.J.5    Cafiso, D.S.6
  • 13
    • 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
    • Faraldo-Gómez JD, Smith GR, Sansom MSP. 2003. Molecular dynamics simulations of the bacterial outer membrane protein FhuA: a comparative study of the ferrichrome-free and bound states. Biophys J 85:1406-1420. http://dx.doi.org/10.1016/S0006-3495(03)74573-1.
    • (2003) Biophys J , vol.85 , pp. 1406-1420
    • Faraldo-Gómez, J.D.1    Smith, G.R.2    Sansom, M.S.P.3
  • 14
    • 0017258036 scopus 로고
    • Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and ϕ80 to Escherichia coli
    • Hancock RW, Braun V. 1976. Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and ϕ80 to Escherichia coli. J Bacteriol 125:409-415.
    • (1976) J Bacteriol , vol.125 , pp. 409-415
    • Hancock, R.W.1    Braun, V.2
  • 15
    • 67651233947 scopus 로고    scopus 로고
    • Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB
    • Ollis AA, Manning M, Held KG, Postle K. 2009. Cytoplasmic membrane protonmotive force energizes periplasmic interactions between ExbD and TonB. Mol Microbiol 73:466-481. http://dx.doi.org/10.1111/j.1365-2958.2009.06785.x.
    • (2009) Mol Microbiol , vol.73 , pp. 466-481
    • Ollis, A.A.1    Manning, M.2    Held, K.G.3    Postle, K.4
  • 16
    • 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, Gunter K, Braun V. 1989. 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 171:5127-5134.
    • (1989) J Bacteriol , vol.171 , pp. 5127-5134
    • Fischer, E.1    Gunter, K.2    Braun, V.3
  • 17
    • 0024730355 scopus 로고
    • Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively
    • Eick-Helmerich K, Braun V. 1989. Import of biopolymers into Escherichia coli: nucleotide sequences of the exbB and exbD genes are homologous to those of the tolQ and tolR genes, respectively. J Bacteriol 171:5117-5126.
    • (1989) J Bacteriol , vol.171 , pp. 5117-5126
    • Eick-Helmerich, K.1    Braun, V.2
  • 18
    • 84880032567 scopus 로고    scopus 로고
    • Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway
    • Baker KR, Postle K. 2013. Mutations in Escherichia coli ExbB transmembrane domains identify scaffolding and signal transduction functions and exclude participation in a proton pathway. J Bacteriol 195:2898-2911. http://dx.doi.org/10.1128/JB.00017-13.
    • (2013) J Bacteriol , vol.195 , pp. 2898-2911
    • Baker, K.R.1    Postle, K.2
  • 19
    • 0026723111 scopus 로고
    • Membrane topology of the Escherichia coli ExbD protein
    • Kampfenkel K, Braun V. 1992. Membrane topology of the Escherichia coli ExbD protein. J Bacteriol 174:5485-5487.
    • (1992) J Bacteriol , vol.174 , pp. 5485-5487
    • Kampfenkel, K.1    Braun, V.2
  • 20
    • 34248636774 scopus 로고    scopus 로고
    • Bioinformatic analysis of the TonB protein family
    • Chu BH, Peacock RS, Vogel H. 2007. Bioinformatic analysis of the TonB protein family. Biometals 20:467-483. http://dx.doi.org/10.1007/s10534-006-9049-4.
    • (2007) Biometals , vol.20 , pp. 467-483
    • Chu, B.H.1    Peacock, R.S.2    Vogel, H.3
  • 21
    • 0027154838 scopus 로고
    • A sequence-specific function for the N-terminal signal-like sequence of the TonB protein
    • Karlsson M, Hannavy K, Higgins CF. 1993. A sequence-specific function for the N-terminal signal-like sequence of the TonB protein. Mol Microbiol 8:379-388. http://dx.doi.org/10.1111/j.1365-2958.1993.tb01581.x.
    • (1993) Mol Microbiol , vol.8 , pp. 379-388
    • Karlsson, M.1    Hannavy, K.2    Higgins, C.F.3
  • 22
    • 80053614487 scopus 로고    scopus 로고
    • Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains
    • Jana B, Manning M, Postle K. 2011. Mutations in the ExbB cytoplasmic carboxy terminus prevent energy-dependent interaction between the TonB and ExbD periplasmic domains. J Bacteriol 193:5649-5657. http://dx.doi.org/10.1128/JB.05674-11.
    • (2011) J Bacteriol , vol.193 , pp. 5649-5657
    • Jana, B.1    Manning, M.2    Postle, K.3
  • 23
    • 84855811875 scopus 로고    scopus 로고
    • ExbD mutants define initial stages in TonB energization
    • Ollis AA, Postle K. 2012. ExbD mutants define initial stages in TonB energization. J Mol Biol 415:237-247. http://dx.doi.org/10.1016/j.jmb.2011.11.005.
    • (2012) J Mol Biol , vol.415 , pp. 237-247
    • Ollis, A.A.1    Postle, K.2
  • 24
    • 35748976227 scopus 로고    scopus 로고
    • The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins
    • Garcia-Herrero A, Peacock RS, Howard SP, Vogel HJ. 2007. The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore-binding proteins. Mol Microbiol 66:872-889. http://dx.doi.org/10.1111/j.1365-2958.2007.05957.x.
    • (2007) Mol Microbiol , vol.66 , pp. 872-889
    • Garcia-Herrero, A.1    Peacock, R.S.2    Howard, S.P.3    Vogel, H.J.4
  • 25
    • 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
  • 26
    • 84855824413 scopus 로고    scopus 로고
    • The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers
    • Ollis AA, Postle K. 2011. The same periplasmic ExbD residues mediate in vivo interactions between ExbD homodimers and ExbD-TonB heterodimers. J Bacteriol 193:6852-6863. http://dx.doi.org/10.1128/JB.06190-11.
    • (2011) J Bacteriol , vol.193 , pp. 6852-6863
    • Ollis, A.A.1    Postle, K.2
  • 27
    • 84864020106 scopus 로고    scopus 로고
    • The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization
    • Ollis AA, Kumar A, Postle K. 2012. The ExbD periplasmic domain contains distinct functional regions for two stages in TonB energization. J Bacteriol 194:3069-3077. http://dx.doi.org/10.1128/JB.00015-12.
    • (2012) J Bacteriol , vol.194 , pp. 3069-3077
    • Ollis, A.A.1    Kumar, A.2    Postle, K.3
  • 28
    • 84864021815 scopus 로고    scopus 로고
    • Identification of functionally important TonBExbD periplasmic domain interactions in vivo
    • Ollis AA, Postle K. 2012. Identification of functionally important TonBExbD periplasmic domain interactions in vivo. J Bacteriol 194:3078-3087. http://dx.doi.org/10.1128/JB.00018-12.
    • (2012) J Bacteriol , vol.194 , pp. 3078-3087
    • Ollis, A.A.1    Postle, K.2
  • 29
    • 84876274460 scopus 로고    scopus 로고
    • Monomeric TonB and the Ton Box are required for the formation of a highaffinity transporter-TonB complex
    • Freed DM, Lukasik SM, Sikora A, Mokdad A, Cafiso DS. 2013. Monomeric TonB and the Ton Box are required for the formation of a highaffinity transporter-TonB complex. Biochemistry 52:2638-2648. http://dx.doi.org/10.1021/bi3016108.
    • (2013) Biochemistry , vol.52 , pp. 2638-2648
    • Freed, D.M.1    Lukasik, S.M.2    Sikora, A.3    Mokdad, A.4    Cafiso, D.S.5
  • 31
    • 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. http://dx.doi.org/10.1126/science.1127694.
    • (2006) Science , vol.312 , pp. 1396-1399
    • Shultis, D.D.1    Purdy, M.D.2    Banchs, C.N.3    Wiener, M.C.4
  • 32
    • 0022931302 scopus 로고
    • Sequenceimposed structural constraints in the TonB protein of E. coli
    • Evans JS, Levine BA, Trayer IP, Dorman CJ, Higgins CF. 1986. Sequenceimposed structural constraints in the TonB protein of E. coli. FEBS Lett 208: 211-216. http://dx.doi.org/10.1016/0014-5793(86)81020-1.
    • (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
  • 33
    • 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. http://dx.doi.org/10.1111/j.1365-2958.1993.tb00966.x.
    • (1993) Mol Microbiol , vol.10 , pp. 943-953
    • Larsen, R.A.1    Wood, G.E.2    Postle, K.3
  • 34
    • 77950282521 scopus 로고    scopus 로고
    • The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria
    • Köhler SD, Weber A, Howard SP, Welte W, Drescher M. 2010. The proline-rich domain of TonB possesses an extended polyproline II-like conformation of sufficient length to span the periplasm of Gram-negative bacteria. Protein Sci 19:625-630. http://dx.doi.org/10.1002/pro.345.
    • (2010) Protein Sci , vol.19 , pp. 625-630
    • Köhler, S.D.1    Weber, A.2    Howard, S.P.3    Welte, W.4    Drescher, M.5
  • 36
    • 0141994975 scopus 로고    scopus 로고
    • Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa
    • Matias VRF, Al-Amoudi A, Dubochet J, Beveridge TJ. 2003. Cryotransmission electron microscopy of frozen-hydrated sections of Escherichia coli and Pseudomonas aeruginosa. J Bacteriol 185:6112-6118. http://dx.doi.org/10.1128/JB.185.20.6112-6118.2003.
    • (2003) J Bacteriol , vol.185 , pp. 6112-6118
    • Matias, V.R.F.1    Al-Amoudi, A.2    Dubochet, J.3    Beveridge, T.J.4
  • 37
    • 0346334403 scopus 로고    scopus 로고
    • Evidence for dynamic clustering of carboxyterminal aromatic amino acids in TonB-dependent energy transduction
    • Ghosh J, Postle K. 2004. Evidence for dynamic clustering of carboxyterminal aromatic amino acids in TonB-dependent energy transduction. Mol Microbiol 51:203-213. http://dx.doi.org/10.1046/j.1365-2958.2003.03816.x.
    • (2004) Mol Microbiol , vol.51 , pp. 203-213
    • Ghosh, J.1    Postle, K.2
  • 39
    • 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. http://dx.doi.org/10.1128/JB.185.19.5747-5754.2003.
    • (2003) J Bacteriol , vol.185 , pp. 5747-5754
    • Sauter, A.1    Howard, S.P.2    Braun, V.3
  • 40
    • 12344263219 scopus 로고    scopus 로고
    • Disulphide trapping of an in vivo energydependent conformation of Escherichia coli TonB protein
    • Ghosh J, Postle K. 2005. Disulphide trapping of an in vivo energydependent conformation of Escherichia coli TonB protein. Mol Microbiol 55:276-288. http://dx.doi.org/10.1111/j.1365-2958.2004.04384.x.
    • (2005) Mol Microbiol , vol.55 , pp. 276-288
    • Ghosh, J.1    Postle, K.2
  • 41
    • 0035045544 scopus 로고    scopus 로고
    • Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA
    • Moeck GS, Letellier L. 2001. Characterization of in vitro interactions between a truncated TonB protein from Escherichia coli and the outer membrane receptors FhuA and FepA. J Bacteriol 183:2755-2764. http://dx.doi.org/10.1128/JB.183.9.2755-2764.2001.
    • (2001) J Bacteriol , vol.183 , pp. 2755-2764
    • Moeck, G.S.1    Letellier, L.2
  • 42
    • 79952158450 scopus 로고    scopus 로고
    • The TonB dimeric crystal structures do not exist in vivo
    • Postle K, Kastead KA, Gresock MG, Ghosh J, Swayne CD. 2010. The TonB dimeric crystal structures do not exist in vivo. mBio 1(5):e00307-10. http://dx.doi.org/10.1128/mBio.00307-10.
    • (2010) mBio , vol.1 , Issue.5
    • Postle, K.1    Kastead, K.A.2    Gresock, M.G.3    Ghosh, J.4    Swayne, C.D.5
  • 43
    • 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. http://dx.doi.org/10.1046/j.1365-2958.1999.01317.x.
    • (1999) Mol Microbiol , vol.31 , pp. 1809-1824
    • Larsen, R.A.1    Thomas, M.G.2    Postle, K.3
  • 44
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs PI, Larsen RA, Postle K. 2002. Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol Microbiol 44:271-281. http://dx.doi.org/10.1046/j.1365-2958.2002.02880.x.
    • (2002) Mol Microbiol , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 45
    • 0018195098 scopus 로고
    • Outer membrane-dependent transport systems in Escherichia coli: turnover of TonB function
    • Kadner RJ, McElhaney G. 1978. Outer membrane-dependent transport systems in Escherichia coli: turnover of TonB function. J Bacteriol 134: 1020-1029.
    • (1978) J Bacteriol , vol.134 , pp. 1020-1029
    • Kadner, R.J.1    McElhaney, G.2
  • 46
    • 84899917848 scopus 로고    scopus 로고
    • Coordinated rearrangements between cytoplasmic and periplasmic domains of the membrane protein complex ExbB-ExbD of Escherichia coli
    • Sverzhinsky A, Fabre L, Cottreau AL, Biot-Pelletier DMP, Khalil S, Bostina M, Rouiller I, Coulton JW. 2014. Coordinated rearrangements between cytoplasmic and periplasmic domains of the membrane protein complex ExbB-ExbD of Escherichia coli. Structure 22:791-797. http://dx.doi.org/10.1016/j.str.2014.02.010.
    • (2014) Structure , vol.22 , pp. 791-797
    • Sverzhinsky, A.1    Fabre, L.2    Cottreau, A.L.3    Biot-Pelletier, D.M.P.4    Khalil, S.5    Bostina, M.6    Rouiller, I.7    Coulton, J.W.8
  • 49
    • 77953627340 scopus 로고    scopus 로고
    • Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions
    • Popot J-L. 2010. Amphipols, nanodiscs, and fluorinated surfactants: three nonconventional approaches to studying membrane proteins in aqueous solutions. Annu Rev Biochem 79:737-775. http://dx.doi.org/10.1146/annurev.biochem.052208.114057.
    • (2010) Annu Rev Biochem , vol.79 , pp. 737-775
    • Popot, J.-L.1
  • 50
    • 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. http://dx.doi.org/10.1074/jbc.M311784200.
    • (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
  • 52
    • 0035574461 scopus 로고    scopus 로고
    • Detection of pET-vector encoded, recombinant S-tagged proteins using the monoclonal antibody ATOM-2
    • Park J-H, Na S-Y, Lee H-H, Lee Y-J, Kim KL. 2001. Detection of pET-vector encoded, recombinant S-tagged proteins using the monoclonal antibody ATOM-2. Hybridoma 20:17-23. http://dx.doi.org/10.1089/027245701300060364.
    • (2001) Hybridoma , vol.20 , pp. 17-23
    • Park, J.-H.1    Na, S.-Y.2    Lee, H.-H.3    Lee, Y.-J.4    Kim, K.L.5
  • 53
    • 33644787225 scopus 로고    scopus 로고
    • Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB
    • Carter DM, Gagnon J-N, Damlaj M, Mandava S, Makowski L, Rodi DJ, Pawelek PD, Coulton JW. 2006. Phage display reveals multiple contact sites between FhuA, an outer membrane receptor of Escherichia coli, and TonB. J Mol Biol 357:236-251. http://dx.doi.org/10.1016/j.jmb.2005.12.039.
    • (2006) J Mol Biol , vol.357 , pp. 236-251
    • Carter, D.M.1    Gagnon, J.-N.2    Damlaj, M.3    Mandava, S.4    Makowski, L.5    Rodi, D.J.6    Pawelek, P.D.7    Coulton, J.W.8
  • 54
    • 2442507626 scopus 로고    scopus 로고
    • RELIC-a bioinformatics server for combinatorial peptide analysis and identification of protein-ligand interaction sites
    • Mandava S, Makowski L, Devarapalli S, Uzubell J, Rodi DJ. 2004. RELIC-a bioinformatics server for combinatorial peptide analysis and identification of protein-ligand interaction sites. Proteomics 4:1439-1460. http://dx.doi.org/10.1002/pmic.200300680.
    • (2004) Proteomics , vol.4 , pp. 1439-1460
    • Mandava, S.1    Makowski, L.2    Devarapalli, S.3    Uzubell, J.4    Rodi, D.J.5
  • 55
    • 84884184827 scopus 로고    scopus 로고
    • Sedimentation velocity analytical ultracentrifugation in hydrogenated and deuterated solvents for the characterization of membrane proteins
    • Roy A, Nury H, Wiseman B, Sarwan J, Jault J-M, Ebel C. 2013. Sedimentation velocity analytical ultracentrifugation in hydrogenated and deuterated solvents for the characterization of membrane proteins. Methods Mol Biol 1033:219-251. http://dx.doi.org/10.1007/978-1-62703-487-6_15.
    • (2013) Methods Mol Biol , vol.1033 , pp. 219-251
    • Roy, A.1    Nury, H.2    Wiseman, B.3    Sarwan, J.4    Jault, J.-M.5    Ebel, C.6
  • 56
    • 33750293579 scopus 로고    scopus 로고
    • Analytical ultracentrifuge for the characterization of detergent in solution
    • Salvay A, Ebel C. 2006. Analytical ultracentrifuge for the characterization of detergent in solution. Prog Colloid Polym Sci 131:74-82. http://dx.doi.org/10.1007/2882_006.
    • (2006) Prog Colloid Polym Sci , vol.131 , pp. 74-82
    • Salvay, A.1    Ebel, C.2
  • 57
    • 0024321837 scopus 로고
    • Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography
    • Hayashi Y, Matsui H, Takagi T. 1989. Membrane protein molecular weight determined by low-angle laser light-scattering photometry coupled with high-performance gel chromatography. Methods Enzymol 172: 514-528. http://dx.doi.org/10.1016/S0076-6879(89)72031-0.
    • (1989) Methods Enzymol , vol.172 , pp. 514-528
    • Hayashi, Y.1    Matsui, H.2    Takagi, T.3
  • 58
    • 79960055093 scopus 로고    scopus 로고
    • Native agarose gel electrophoresis of multiprotein complexes
    • Kim R. 2011. Native agarose gel electrophoresis of multiprotein complexes. Cold Spring Harb Protoc 2011:884-887. http://dx.doi.org/10.1101/pdb.prot4558.
    • (2011) Cold Spring Harb Protoc , vol.2011 , pp. 884-887
    • Kim, R.1
  • 60
    • 47349120456 scopus 로고    scopus 로고
    • Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements
    • Jachimska B, Wasilewska M, Adamczyk Z. 2008. Characterization of globular protein solutions by dynamic light scattering, electrophoretic mobility, and viscosity measurements. Langmuir 24:6866-6872. http://dx.doi.org/10.1021/la800548p.
    • (2008) Langmuir , vol.24 , pp. 6866-6872
    • Jachimska, B.1    Wasilewska, M.2    Adamczyk, Z.3
  • 61
    • 33845316126 scopus 로고    scopus 로고
    • Automated acquisition of electron microscopic random conical tilt sets
    • Zheng SQ, Kollman JM, Braunfeld MB, Sedat JW, Agard DA. 2007. Automated acquisition of electron microscopic random conical tilt sets. J Struct Biol 157:148-155. http://dx.doi.org/10.1016/j.jsb.2006.10.026.
    • (2007) J Struct Biol , vol.157 , pp. 148-155
    • Zheng, S.Q.1    Kollman, J.M.2    Braunfeld, M.B.3    Sedat, J.W.4    Agard, D.A.5
  • 62
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell JA, Grigorieff N. 2003. Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-347. http://dx.doi.org/10.1016/S1047-8477(03)00069-8.
    • (2003) J Struct Biol , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 63
    • 44949165726 scopus 로고    scopus 로고
    • Image processing for electron microscopy single-particle analysis using XMIPP
    • Scheres SHW, Nunez-Ramirez R, Sorzano COS, Carazo JM, Marabini R. 2008. Image processing for electron microscopy single-particle analysis using XMIPP. Nat Protoc 3:977-990. http://dx.doi.org/10.1038/nprot.2008.62.
    • (2008) Nat Protoc , vol.3 , pp. 977-990
    • Scheres, S.H.W.1    Nunez-Ramirez, R.2    Sorzano, C.O.S.3    Carazo, J.M.4    Marabini, R.5
  • 65
    • 84985231782 scopus 로고
    • Threedimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J. 1987. Threedimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146(Part 2):113-136. http://dx.doi.org/10.1111/j.1365-2818.1987.tb01333.x.
    • (1987) J Microsc , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 66
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, Ludtke SJ. 2007. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. http://dx.doi.org/10.1016/j.jsb.2006.05.009.
    • (2007) J Struct Biol , vol.157 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6    Ludtke, S.J.7
  • 67
    • 84863011784 scopus 로고    scopus 로고
    • Iterative stable alignment and clustering of 2D transmission electron microscope images
    • Yang Z, Fang J, Chittuluru J, Asturias FJ, Penczek PA. 2012. Iterative stable alignment and clustering of 2D transmission electron microscope images. Structure 20:237-247. http://dx.doi.org/10.1016/j.str.2011.12.007.
    • (2012) Structure , vol.20 , pp. 237-247
    • Yang, Z.1    Fang, J.2    Chittuluru, J.3    Asturias, F.J.4    Penczek, P.A.5
  • 68
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SHW. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530. http://dx.doi.org/10.1016/j.jsb.2012.09.006.
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.W.1
  • 70
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Harpaz Y, Gerstein M, Chothia C. 1994. Volume changes on protein folding. Structure 2:641-649. http://dx.doi.org/10.1016/S0969-2126(00)00065-4.
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 71
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres SHW, Chen S. 2012. Prevention of overfitting in cryo-EM structure determination. Nat Methods 9:853-854. http://dx.doi.org/10.1038/nmeth.2115.
    • (2012) Nat Methods , vol.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 72
    • 0018388886 scopus 로고
    • Identification of the Escherichia coli tonB gene product in minicells containing tonB hybrid plasmids
    • Postle K, Reznikoff WS. 1979. Identification of the Escherichia coli tonB gene product in minicells containing tonB hybrid plasmids. J Mol Biol 131:619-636. http://dx.doi.org/10.1016/0022-2836(79)90011-1.
    • (1979) J Mol Biol , vol.131 , pp. 619-636
    • Postle, K.1    Reznikoff, W.S.2
  • 73
    • 55649088213 scopus 로고    scopus 로고
    • Static light scattering to characterize membrane proteins in detergent solution
    • Slotboom DJ, Duurkens RH, Olieman K, Erkens GB. 2008. Static light scattering to characterize membrane proteins in detergent solution. Methods 46:73-82. http://dx.doi.org/10.1016/j.ymeth.2008.06.012.
    • (2008) Methods , vol.46 , pp. 73-82
    • Slotboom, D.J.1    Duurkens, R.H.2    Olieman, K.3    Erkens, G.B.4
  • 74
    • 0030571043 scopus 로고    scopus 로고
    • Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions
    • Wen J, Arakawa T, Philo JS. 1996. Size-exclusion chromatography with on-line light-scattering, absorbance, and refractive index detectors for studying proteins and their interactions. Anal Biochem 240:155-166. http://dx.doi.org/10.1006/abio.1996.0345.
    • (1996) Anal Biochem , vol.240 , pp. 155-166
    • Wen, J.1    Arakawa, T.2    Philo, J.S.3
  • 75
    • 0025332506 scopus 로고
    • Aerobic regulation of the Escherichia coli tonB gene by changes in iron availability and the fur locus
    • Postle K. 1990. Aerobic regulation of the Escherichia coli tonB gene by changes in iron availability and the fur locus. J Bacteriol 172:2287-2293.
    • (1990) J Bacteriol , vol.172 , pp. 2287-2293
    • Postle, K.1
  • 76
    • 41549103706 scopus 로고    scopus 로고
    • Visualization of interactions between siderophore transporters and the energizing protein TonB by native PAGE
    • Choul-Li S, Adams H, Pattus F, Celia H. 2008. Visualization of interactions between siderophore transporters and the energizing protein TonB by native PAGE. Electrophoresis 29:1333-1338. http://dx.doi.org/10.1002/elps.200700612.
    • (2008) Electrophoresis , vol.29 , pp. 1333-1338
    • Choul-Li, S.1    Adams, H.2    Pattus, F.3    Celia, H.4
  • 77
    • 44349149922 scopus 로고    scopus 로고
    • Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane
    • Kaserer WA, Jiang X, Xiao Q, Scott DC, Bauler M, Copeland D, Newton SMC, Klebba PE. 2008. Insight from TonB hybrid proteins into the mechanism of iron transport through the outer membrane. J Bacteriol 190:4001-4016. http://dx.doi.org/10.1128/JB.00135-08.
    • (2008) J Bacteriol , vol.190 , pp. 4001-4016
    • Kaserer, W.A.1    Jiang, X.2    Xiao, Q.3    Scott, D.C.4    Bauler, M.5    Copeland, D.6    Newton, S.M.C.7    Klebba, P.E.8
  • 78
    • 0026344184 scopus 로고
    • Evidence for a TonB-dependent energy transduction complex in Escherichia coli
    • Skare JT, Postle K. 1991. Evidence for a TonB-dependent energy transduction complex in Escherichia coli. Mol Microbiol 5:2883-2890. http://dx.doi.org/10.1111/j.1365-2958.1991.tb01848.x.
    • (1991) Mol Microbiol , vol.5 , pp. 2883-2890
    • Skare, J.T.1    Postle, K.2
  • 79
    • 0029117190 scopus 로고
    • Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability
    • Ahmer BM, Thomas MG, Larsen RA, Postle K. 1995. Characterization of the exbBD operon of Escherichia coli and the role of ExbB and ExbD in TonB function and stability. J Bacteriol 177:4742-4747.
    • (1995) J Bacteriol , vol.177 , pp. 4742-4747
    • Ahmer, B.M.1    Thomas, M.G.2    Larsen, R.A.3    Postle, K.4
  • 80
    • 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. 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    Killmann, H.5    Traub, I.6
  • 81
    • 33845939047 scopus 로고    scopus 로고
    • Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization
    • Scheres SHW, Gao H, Valle M, Herman G, Eggermont J, Frank J, Carazo J-M. 2007. Disentangling conformational states of macromolecules in 3D-EM through likelihood optimization. Nat Methods 4:27-29. http://dx.doi.org/10.1038/nmeth992.
    • (2007) Nat Methods , vol.4 , pp. 27-29
    • Scheres, S.H.W.1    Gao, H.2    Valle, M.3    Herman, G.4    Eggermont, J.5    Frank, J.6    Carazo, J.-M.7
  • 82
    • 79959668319 scopus 로고    scopus 로고
    • Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects
    • Glaeser RM, Hall RJ. 2011. Reaching the information limit in cryo-EM of biological macromolecules: experimental aspects. Biophys J 100:2331-2337. http://dx.doi.org/10.1016/j.bpj.2011.04.018.
    • (2011) Biophys J , vol.100 , pp. 2331-2337
    • Glaeser, R.M.1    Hall, R.J.2
  • 83
    • 4744344736 scopus 로고    scopus 로고
    • Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs
    • Orlova EV, Saibil HR. 2004. Structure determination of macromolecular assemblies by single-particle analysis of cryo-electron micrographs. Curr Opin Struct Biol 14:584-590. http://dx.doi.org/10.1016/j.sbi.2004.08.004.
    • (2004) Curr Opin Struct Biol , vol.14 , pp. 584-590
    • Orlova, E.V.1    Saibil, H.R.2
  • 84
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification-powerful tools in modern electron microscopy
    • Ohi M, Li Y, Cheng Y, Walz T. 2004. Negative staining and image classification-powerful tools in modern electron microscopy. Biol Proced Online 6:23-34. http://dx.doi.org/10.1251/bpo70.
    • (2004) Biol Proced Online , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 85
    • 34447339675 scopus 로고    scopus 로고
    • Mechanics of force propagation in TonB-dependent outer membrane transport
    • Gumbart J, Wiener MC, Tajkhorshid E. 2007. Mechanics of force propagation in TonB-dependent outer membrane transport. Biophys J 93: 496-504. http://dx.doi.org/10.1529/biophysj.107.104158.
    • (2007) Biophys J , vol.93 , pp. 496-504
    • Gumbart, J.1    Wiener, M.C.2    Tajkhorshid, E.3
  • 86
    • 0027474991 scopus 로고
    • Left-handed polyproline II helices commonly occur in globular proteins
    • Adzhubei AA, Sternberg MJE. 1993. Left-handed polyproline II helices commonly occur in globular proteins. J Mol Biol 229:472-493. http://dx.doi.org/10.1006/jmbi.1993.1047.
    • (1993) J Mol Biol , vol.229 , pp. 472-493
    • Adzhubei, A.A.1    Sternberg, M.J.E.2
  • 87
    • 12944281484 scopus 로고    scopus 로고
    • On the stability of polyproline-I and II structures of proline oligopeptides
    • Kakinoki S, Hirano Y, Oka M. 2005. On the stability of polyproline-I and II structures of proline oligopeptides. Polym Bull 53:109-115. http://dx.doi.org/10.1007/s00289-004-0317-6.
    • (2005) Polym Bull , vol.53 , pp. 109-115
    • Kakinoki, S.1    Hirano, Y.2    Oka, M.3
  • 88
    • 33947424588 scopus 로고    scopus 로고
    • His20 provides the sole functionally significant side chain in the essential TonB transmembrane domain
    • Larsen RA, Deckert GE, Kastead KA, Devanathan S, Keller KL, Postle K. 2007. His20 provides the sole functionally significant side chain in the essential TonB transmembrane domain. J Bacteriol 189:2825-2833. http://dx.doi.org/10.1128/JB.01925-06.
    • (2007) J Bacteriol , vol.189 , pp. 2825-2833
    • Larsen, R.A.1    Deckert, G.E.2    Kastead, K.A.3    Devanathan, S.4    Keller, K.L.5    Postle, K.6
  • 89
    • 84897000286 scopus 로고    scopus 로고
    • The resolution revolution
    • Kühlbrandt W. 2014. The resolution revolution. Science 343:1443-1444. http://dx.doi.org/10.1126/science.1251652.
    • (2014) Science , vol.343 , pp. 1443-1444
    • Kühlbrandt, W.1
  • 91
    • 84889607320 scopus 로고    scopus 로고
    • Structure of the TRPV1 ion channel determined by electron cryo-microscopy
    • Liao M, Erhu C, Julius D, Cheng T. 2013. Structure of the TRPV1 ion channel determined by electron cryo-microscopy. Nature 504:107-112. http://dx.doi.org/10.1038/nature12822.
    • (2013) Nature , vol.504 , pp. 107-112
    • Liao, M.1    Erhu, C.2    Julius, D.3    Cheng, T.4
  • 92
    • 0034818457 scopus 로고    scopus 로고
    • TonB-dependent systems of uropathogenic Escherichia coli: aerobactin and heme transport and TonB are required for virulence in the mouse
    • Torres AG, Redford P, Welch RA, Payne SM. 2001. TonB-dependent systems of uropathogenic Escherichia coli: aerobactin and heme transport and TonB are required for virulence in the mouse. Infect Immun 69:6179-6185. http://dx.doi.org/10.1128/IAI.69.10.6179-6185.2001.
    • (2001) Infect Immun , vol.69 , pp. 6179-6185
    • Torres, A.G.1    Redford, P.2    Welch, R.A.3    Payne, S.M.4
  • 93
    • 84899769431 scopus 로고    scopus 로고
    • Inhibitors of TonB function identified by a high-throughput screen for inhibitors of iron acquisition in uropathogenic Escherichia coli CFT073
    • Yep A, McQuade T, Kirchhoff P, Larsen M, Mobley HLT. 2014. Inhibitors of TonB function identified by a high-throughput screen for inhibitors of iron acquisition in uropathogenic Escherichia coli CFT073. mBio 5(2):e01089-13. http://dx.doi.org/10.1128/mBio.01089-13.
    • (2014) mBio , vol.5 , Issue.2
    • Yep, A.1    McQuade, T.2    Kirchhoff, P.3    Larsen, M.4    Mobley, H.L.T.5

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