메뉴 건너뛰기




Volumn 8, Issue SUPPL., 2003, Pages

Three paradoxes of ferric enterobactin uptake

Author keywords

Bioenergetics; FepA; Ferric enterobactin; Metal Transport; Outer Membrane; Review; TonB

Indexed keywords

BACTERIAL PROTEIN; ENTEROCHELIN; IRON BINDING PROTEIN; IRON CHELATE; LIGAND; OUTER MEMBRANE PROTEIN; FERRIC ION; ION CHANNEL;

EID: 3142688448     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/1233     Document Type: Review
Times cited : (36)

References (29)
  • 2
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A. D., E. Hofmann, J. W. Coulton, K. Diederichs, and W. Welte: Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282, 2215-20 (1998)
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 3
    • 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, K. P., 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, 771-8 (1998)
    • (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
  • 5
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento, D. P., A. K. Mohanty, R. J. Kadner, and M. C. Wiener: Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat Struct Biol 10, 394-401 (2003)
    • (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
  • 6
    • 0033770845 scopus 로고    scopus 로고
    • Aromatic components of two ferric enterobactin binding sites in Escherichia coli FepA
    • Cao, Z., Z. Qi, C. Sprencel, S. M. Newton, and P. E. Klebba: Aromatic components of two ferric enterobactin binding sites in Escherichia coli FepA. Mol Microbiol 37, 1306-17 (2000)
    • (2000) Mol Microbiol , vol.37 , pp. 1306-1317
    • Cao, Z.1    Qi, Z.2    Sprencel, C.3    Newton, S.M.4    Klebba, P.E.5
  • 7
    • 0035918333 scopus 로고    scopus 로고
    • Exchangeability of N termini in the ligand-gated porins of Escherichia coli
    • Scott, D. C., Z. Cao, Z. Qi, M. Bauler, J. D. Igo, S. M. Newton, and P. E. Klebba: Exchangeability of N termini in the ligand-gated porins of Escherichia coli. J Biol Chem. 276, 13025-33 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 13025-13033
    • Scott, D.C.1    Cao, Z.2    Qi, Z.3    Bauler, M.4    Igo, J.D.5    Newton, S.M.6    Klebba, P.E.7
  • 9
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • Merianos, H. J., 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, 205-9 (2000)
    • (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
  • 10
    • 0035845572 scopus 로고    scopus 로고
    • The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain
    • Usher, K. C., E. Ozkan, K. H. Gardner, and J. Deisenhofer: The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain Proc Natl Acad Sci U S A 98, 10676-81 (2001)
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 10676-10681
    • Usher, K.C.1    Ozkan, E.2    Gardner, K.H.3    Deisenhofer, J.4
  • 11
    • 0037428446 scopus 로고    scopus 로고
    • Spectroscopic observations of ferric enterobactin transport
    • Cao, Z., P. Warfel, S. M. Newton, and P. E. Klebba: Spectroscopic observations of ferric enterobactin transport. J Biol Chem 278, 29-38 (2002)
    • (2002) J Biol Chem , vol.278 , pp. 29-38
    • Cao, Z.1    Warfel, P.2    Newton, S.M.3    Klebba, P.E.4
  • 12
    • 3142681156 scopus 로고    scopus 로고
    • Doctoral thesis, University of Oklahoma
    • Scott, D. C. : Doctoral thesis, University of Oklahoma (2001)
    • (2001)
    • Scott, D.C.1
  • 13
    • 0032831642 scopus 로고    scopus 로고
    • The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli
    • Braun, M., H. Killmann, and V. Braun: The beta-barrel domain of FhuADelta5-160 is sufficient for TonB-dependent FhuA activities of Escherichia coli Mol Microbiol. 33, 1037-49 (1999)
    • (1999) Mol Microbiol , vol.33 , pp. 1037-1049
    • Braun, M.1    Killmann, H.2    Braun, V.3
  • 14
    • 0036778139 scopus 로고    scopus 로고
    • FepA with globular domain deletions lacks activity
    • Vakharia, H. L., and K. Postle: FepA with globular domain deletions lacks activity. J Bacteriol 184, 5508-12 (2002)
    • (2002) J Bacteriol , vol.184 , pp. 5508-5512
    • Vakharia, H.L.1    Postle, K.2
  • 15
    • 0032034801 scopus 로고    scopus 로고
    • Mechanisms of solute transport through outer membrane porins: Burning down the house
    • Klebba, P. E., and S. M. Newton: Mechanisms of solute transport through outer membrane porins: burning down the house. Curr Opin Microbiol 1, 238-247 (1998).
    • (1998) Curr Opin Microbiol , vol.1 , pp. 238-247
    • Klebba, P.E.1    Newton, S.M.2
  • 16
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope
    • Klebba, P. E., J. M. Rutz, J. Liu, and C. K. Murphy: Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J Bioenerg Biomembr 25, 603-11 (1993)
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 17
    • 3142752974 scopus 로고    scopus 로고
    • Site-directed mutagenesis of BtuB TonB boxes and its effect on Vitamin B12 uptake in Escherichia coli
    • ASM, Chicago, Illinois
    • Phan, P. G., N. Cadieux, and R. J. Kadner: Site-directed mutagenesis of BtuB TonB boxes and its effect on Vitamin B12 uptake in Escherichia coli, p. 427. 99th General Meeting of the American Society for Microbiology. ASM, Chicago, Illinois (1999).
    • (1999) 99th General Meeting of the American Society for Microbiology , pp. 427
    • Phan, P.G.1    Cadieux, N.2    Kadner, R.J.3
  • 18
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli
    • published erratum appears in Mol Microbiol 25, 617 (1997)
    • Letain, T. E., and K. Postle: TonB protein appears to transduce energy by shuttling between the cytoplasmic membrane and the outer membrane in Escherichia coli [published erratum appears in Mol Microbiol 25, 617 (1997)] Mol Microbiol 24, 271-83 (1997)
    • (1997) Mol Microbiol , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 19
    • 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., 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 U S A 96, 10673-8 (1999)
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 10673-10678
    • Cadieux, N.1    Kadner, R.J.2
  • 20
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs, P. I., R. A. Larsen, and K. Postle: Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol Microbiol 44, 271-81 (2002)
    • (2002) Mol Microbiol , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 21
    • 0035920228 scopus 로고    scopus 로고
    • Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold
    • Chang, C., A. Mooser, A. Pluckthun, and A. Wlodawer: Crystal structure of the dimeric C-terminal domain of TonB reveals a novel fold J Biol Chem 276:27535-40 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 27535-27540
    • Chang, C.1    Mooser, A.2    Pluckthun, A.3    Wlodawer, A.4
  • 22
    • 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., C. Sanz, A. Shah, J. G. Grossmann, K. Mizuguchi, R. N. Perham, and B. Luisi: Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein. EMBO J 21, 4207-18 (2002).
    • (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
  • 23
    • 0035163972 scopus 로고    scopus 로고
    • The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
    • Cascales, E., R. Lloubes, and J. N. Sturgis: The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB. Mol Microbiol 42, 795-807 (2001)
    • (2001) Mol Microbiol , vol.42 , pp. 795-807
    • Cascales, E.1    Lloubes, R.2    Sturgis, J.N.3
  • 24
    • 0033744772 scopus 로고    scopus 로고
    • Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the ToIA protein
    • Gaspar, J. A., J. A. Thomas, C. L. Marolda, and M. A. Valvano: Surface expression of O-specific lipopolysaccharide in Escherichia coli requires the function of the ToIA protein. Mol Microbiol 38, 262-75 (2000)
    • (2000) Mol Microbiol , vol.38 , pp. 262-275
    • Gaspar, J.A.1    Thomas, J.A.2    Marolda, C.L.3    Valvano, M.A.4
  • 25
    • 0037064287 scopus 로고    scopus 로고
    • TonB-dependent receptors-structural perspectives
    • Ferguson, A. D., and J. Deisenhofer: TonB-dependent receptors-structural perspectives. Biochim Biophys Acta 1565, 318-32 (2002
    • (2002) Biochim Biophys Acta , vol.1565 , pp. 318-332
    • Ferguson, A.D.1    Deisenhofer, J.2
  • 26
    • 0027280517 scopus 로고
    • The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli
    • Bradbeer, C: The proton motive force drives the outer membrane transport of cobalamin in Escherichia coli J Bacteriol 175, 3146-50 (1993)
    • (1993) J Bacteriol , vol.175 , pp. 3146-3150
    • Bradbeer, C.1
  • 27
    • 0017258036 scopus 로고
    • Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli
    • Hancock, R. W., and V. Braun: Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and phi80 to Escherichia coli. J Bacteriol 125, 409-15 (1976)
    • (1976) J Bacteriol , vol.125 , pp. 409-415
    • Hancock, R.W.1    Braun, V.2
  • 28
    • 0017642455 scopus 로고
    • Uptake of ferrienterochelin by Escherichia coli: Energy dependent stage of uptake
    • Pugsley, A. P., and P. Reeves: Uptake of ferrienterochelin by Escherichia coli: energy dependent stage of uptake. J Bacteriol 130, 26-36 (1977)
    • (1977) J Bacteriol , vol.130 , pp. 26-36
    • Pugsley, A.P.1    Reeves, P.2
  • 29
    • 0035980267 scopus 로고    scopus 로고
    • Conformational change in the stator of the bacterial flagellar motor
    • Kojima, S., and D. F. Blair: Conformational change in the stator of the bacterial flagellar motor. Biochemistry 40, 13041-50 (2001)
    • (2001) Biochemistry , vol.40 , pp. 13041-13050
    • Kojima, S.1    Blair, D.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.