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Volumn 65, Issue 2, 2007, Pages 441-453

Studies on colicin B translocation: FepA is gated by TonB

Author keywords

[No Author keywords available]

Indexed keywords

COLICIN B; CYSTEINE; CYTOPLASM PROTEIN; EXBB PROTEIN; OUTER MEMBRANE PROTEIN; PROTEIN EXBD; PROTEIN FEPA; PROTEIN TONB; TOXIN; UNCLASSIFIED DRUG;

EID: 34447339934     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2007.05808.x     Document Type: Article
Times cited : (42)

References (56)
  • 1
    • 0027204861 scopus 로고
    • The wild-type allele of tonB. Escherichia coli is dominant over the tonB1 allele, encoding TonBQ160K, which suppresses the btub451 mutation
    • Anton, M. Heller, K.J. (1993) The wild-type allele of tonB. Escherichia coli is dominant over the tonB1 allele, encoding TonBQ160K, which suppresses the btub451 mutation. Mol Gen Genet 239 : 371 377.
    • (1993) Mol Gen Genet , vol.239 , pp. 371-377
    • Anton, M.1    Heller, K.J.2
  • 2
    • 0031718525 scopus 로고    scopus 로고
    • Displacement of OmpF loop 3 is not required for the membrane translocation of colicins N and a in vivo
    • Bainbridge, G., Armstrong, G.A., Dover, L.G., Whelan, K.F. Lakey, J.H. (1998) Displacement of OmpF loop 3 is not required for the membrane translocation of colicins N and A in vivo. FEBS Lett 432 : 117 122.
    • (1998) FEBS Lett , vol.432 , pp. 117-122
    • Bainbridge, G.1    Armstrong, G.A.2    Dover, L.G.3    Whelan, K.F.4    Lakey, J.H.5
  • 3
    • 0034888050 scopus 로고    scopus 로고
    • Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport
    • Barnard, T.J., Watson, M.E., Jr. McIntosh, M.A. (2001) Mutations in the Escherichia coli receptor FepA reveal residues involved in ligand binding and transport. Mol Microbiol 41 : 527 536.
    • (2001) Mol Microbiol , vol.41 , pp. 527-536
    • Barnard, T.J.1    Watson Jr., M.E.2    McIntosh, M.A.3
  • 4
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates direct interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell, P.E., Nau, C.D., Brown, J.T., Konisky, J. Kadner, R.J. (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
  • 5
    • 0042838110 scopus 로고    scopus 로고
    • In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12
    • Braun, M., Endriss, F., Killmann, H. Braun, V. (2003) In vivo reconstitution of the FhuA transport protein of Escherichia coli K-12. J Bacteriol 185 : 5508 5518.
    • (2003) J Bacteriol , vol.185 , pp. 5508-5518
    • Braun, M.1    Endriss, F.2    Killmann, H.3    Braun, V.4
  • 6
    • 0034471897 scopus 로고    scopus 로고
    • Iron transport in Escherichia coli. Crystal structure of FhuA, an outer membrane iron and antibiotic transporter
    • Braun, V., Braun, M. Killmann, H. (2000) Iron transport in Escherichia coli. Crystal structure of FhuA, an outer membrane iron and antibiotic transporter. Adv Exp Med Biol 485 : 33 43.
    • (2000) Adv Exp Med Biol , vol.485 , pp. 33-43
    • Braun, V.1    Braun, M.2    Killmann, H.3
  • 7
    • 0027501795 scopus 로고
    • Molecular characterization of the Enterobacter aerogenes tonB gene: Identification of a novel type of 'TonB-box' suppressor mutant
    • Bruske, A.K. Heller, K.J. (1993) Molecular characterization of the Enterobacter aerogenes tonB gene: identification of a novel type of 'TonB-box' suppressor mutant. J Bacteriol 175 : 6158 6168.
    • (1993) J Bacteriol , vol.175 , pp. 6158-6168
    • Bruske, A.K.1    Heller, K.J.2
  • 8
  • 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, R.J. (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
  • 10
    • 0141703294 scopus 로고    scopus 로고
    • Differential substrate-induced signaling through the TonB-dependent transporter BtuB
    • Cadieux, N., Phan, P.G., Cafiso, D.S. Kadner, R.J. (2003) Differential substrate-induced signaling through the TonB-dependent transporter BtuB. Proc Natl Acad Sci USA 100 : 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
  • 11
    • 33845951159 scopus 로고    scopus 로고
    • Interactions between TonB from Escherichia coli and the periplasmic protein FhuD
    • Carter, D.M., Miousse, I.R., Gagnon, J.N., Martinez, E., Clements, A., Lee, J., et al. (2006) Interactions between TonB from Escherichia coli and the periplasmic protein FhuD. J Biol Chem 281 : 35413 35424.
    • (2006) J Biol Chem , vol.281 , pp. 35413-35424
    • Carter, D.M.1    Miousse, I.R.2    Gagnon, J.N.3    Martinez, E.4    Clements, A.5    Lee, J.6
  • 13
    • 34248634581 scopus 로고    scopus 로고
    • Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins of Escherichia coli
    • Chakraborty, R., Storey, E. van der Helm, D. (2006) Molecular mechanism of ferricsiderophore passage through the outer membrane receptor proteins of Escherichia coli. Biometals 20 : 263 274.
    • (2006) Biometals , vol.20 , pp. 263-274
    • Chakraborty, R.1    Storey, E.2    Van Der Helm, D.3
  • 14
    • 33750965918 scopus 로고    scopus 로고
    • In meso structure of the cobalamin transporter, BtuB, at 1.95 a resolution
    • Cherezov, V., Yamashita, E., Liu, W., Zhalnina, M., Cramer, W.A. Caffrey, M. (2006) In meso structure of the cobalamin transporter, BtuB, at 1.95 A resolution. J Mol Biol 364 : 716 734.
    • (2006) J Mol Biol , vol.364 , pp. 716-734
    • Cherezov, V.1    Yamashita, E.2    Liu, W.3    Zhalnina, M.4    Cramer, W.A.5    Caffrey, M.6
  • 15
    • 0242670022 scopus 로고    scopus 로고
    • Substrate-induced transmembrane signaling in the cobalamin transporter BtuB
    • Chimento, D.P., Mohanty, A.K., Kadner, R.J. Wiener, M.C. (2003) Substrate-induced transmembrane signaling in the cobalamin transporter BtuB. Nat Struct Biol 10 : 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
  • 16
    • 16344373729 scopus 로고    scopus 로고
    • Comparative structural analysis of TonB-dependent outer membrane transporters: Implications for the transport cycle
    • Chimento, D.P., Kadner, R.J. Wiener, M.C. (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    Wiener, M.C.3
  • 17
    • 14144255323 scopus 로고    scopus 로고
    • The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution
    • Cobessi, D., Celia, H., Folschweiller, N., Schalk, I.J., Abdallah, M.A. Pattus, F. (2005a) The crystal structure of the pyoverdine outer membrane receptor FpvA from Pseudomonas aeruginosa at 3.6 angstroms resolution. J Mol Biol 347 : 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
  • 18
    • 24644432870 scopus 로고    scopus 로고
    • Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa
    • Cobessi, D., Celia, H. Pattus, F. (2005b) Crystal structure at high resolution of ferric-pyochelin and its membrane receptor FptA from Pseudomonas aeruginosa. J Mol Biol 352 : 893 904.
    • (2005) J Mol Biol , vol.352 , pp. 893-904
    • Cobessi, D.1    Celia, H.2    Pattus, F.3
  • 19
    • 0035923423 scopus 로고    scopus 로고
    • Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter
    • Coggshall, K.A., Cadieux, N., Piedmont, C., Kadner, R.J. Cafiso, D.S. (2001) Transport-defective mutations alter the conformation of the energy-coupling motif of an outer membrane transporter. Biochemistry 40 : 13964 13971.
    • (2001) Biochemistry , vol.40 , pp. 13964-13971
    • Coggshall, K.A.1    Cadieux, N.2    Piedmont, C.3    Kadner, R.J.4    Cafiso, D.S.5
  • 20
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of charomosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. Wanner, B. (2000) One-step inactivation of charomosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97 : 6640 6645.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.1    Wanner, B.2
  • 21
    • 24044525255 scopus 로고    scopus 로고
    • Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains
    • Eisenhauer, H.A., Shames, S., Pawelek, P.D. Coulton, J.W. (2005) Siderophore transport through Escherichia coli outer membrane receptor FhuA with disulfide-tethered cork and barrel domains. J Biol Chem 280 : 30574 30580.
    • (2005) J Biol Chem , vol.280 , pp. 30574-30580
    • Eisenhauer, H.A.1    Shames, S.2    Pawelek, P.D.3    Coulton, J.W.4
  • 22
    • 0043165150 scopus 로고    scopus 로고
    • Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity
    • Endriss, F., Braun, M., Killmann, H. Braun, V. (2003) Mutant analysis of the Escherichia coli FhuA protein reveals sites of FhuA activity. J Bacteriol 185 : 4683 4692.
    • (2003) J Bacteriol , vol.185 , pp. 4683-4692
    • Endriss, F.1    Braun, M.2    Killmann, H.3    Braun, V.4
  • 23
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A.D., Hofmann, E., Coulton, J.W., Diederichs, 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    Diederichs, K.4    Welte, W.5
  • 25
    • 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
  • 26
    • 0015633255 scopus 로고
    • Excretion of enterochelin by exbA and exbB mutants of Escherichia coli
    • Gutermann, S.K. Dann, L. (1973) Excretion of enterochelin by exbA and exbB mutants of Escherichia coli. J Bacteriol 114 : 1225 1230.
    • (1973) J Bacteriol , vol.114 , pp. 1225-1230
    • Gutermann, S.K.1    Dann, L.2
  • 27
    • 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.J., Kadner, R.J. 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.J.1    Kadner, R.J.2    Günter, K.3
  • 29
    • 0031791530 scopus 로고    scopus 로고
    • Interactions in the TonB-dependent energy transduction complex: ExbB and ExbD form homomultimers
    • Higgs, P.I., Myers, P.S. 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
  • 30
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB-dependent energy transduction system: TonB, ExbB, ExbD, and FepA
    • Higgs, P.I., Larsen, R.A. Postle, K. (2002) 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
  • 31
    • 0019639160 scopus 로고
    • Inversions between ribosomal RNA genes of Escherichia coli
    • Hill, C.W. Harnish, B.W. (1981) Inversions between ribosomal RNA genes of Escherichia coli. Proc Natl Acad Sci USA 78 : 7069 7072.
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 7069-7072
    • Hill, C.W.1    Harnish, B.W.2
  • 32
    • 1242297815 scopus 로고    scopus 로고
    • Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 a resolution
    • Hilsenbeck, J.L., Park, H., Chen, G., Youn, B., Postle, K. Kang, C. (2004) Crystal structure of the cytotoxic bacterial protein colicin B at 2.5 A resolution. Mol Microbiol 51 : 711 720.
    • (2004) Mol Microbiol , vol.51 , pp. 711-720
    • Hilsenbeck, J.L.1    Park, H.2    Chen, G.3    Youn, B.4    Postle, K.5    Kang, C.6
  • 33
    • 0030926805 scopus 로고    scopus 로고
    • Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria
    • Jiang, X., Payne, M.A., Cao, Z., Foster, S.B., Feix, J.B., Newton, S.M.C. Klebba, P.E. (1997) Ligand-specific opening of a gated-porin channel in the outer membrane of living bacteria. Science 276 : 1261 1264.
    • (1997) Science , vol.276 , pp. 1261-1264
    • Jiang, X.1    Payne, M.A.2    Cao, Z.3    Foster, S.B.4    Feix, J.B.5    Newton, S.M.C.6    Klebba, P.E.7
  • 34
    • 0029116515 scopus 로고
    • Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function
    • Kadner, R.J. Heller, K.J. (1995) Mutual inhibition of cobalamin and siderophore uptake systems suggests their competition for TonB function. J Bacteriol 177 : 4829 4835.
    • (1995) J Bacteriol , vol.177 , pp. 4829-4835
    • Kadner, R.J.1    Heller, K.J.2
  • 35
    • 33646202285 scopus 로고    scopus 로고
    • Solutes modify a conformational transition in a membrane transport protein
    • Kim, M., Xu, Q., Fanucci, G.E. Cafiso, D.S. (2006) Solutes modify a conformational transition in a membrane transport protein. Biophys J 90 : 2922 2929.
    • (2006) Biophys J , vol.90 , pp. 2922-2929
    • Kim, M.1    Xu, Q.2    Fanucci, G.E.3    Cafiso, D.S.4
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 : 680 685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 0028145355 scopus 로고
    • Partial suppression of an Escherichia coli TonB transmembrane domain mutation (ΔV17) by a missense mutation in ExbB
    • Larsen, R.A., Thomas, M.T., Wood, G.E. 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
  • 38
    • 0032991467 scopus 로고    scopus 로고
    • Protonmotive force, ExbB and ligand-bound FepA drive conformational changes in TonB
    • Larsen, R.A., Thomas, M.G. 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
  • 39
    • 0041402639 scopus 로고    scopus 로고
    • Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB
    • Larsen, R.A., Chen, G.J. Postle, K. (2003a) Performance of standard phenotypic assays for TonB activity, as evaluated by varying the level of functional, wild-type TonB. J Bacteriol 185 : 4699 4706.
    • (2003) J Bacteriol , vol.185 , pp. 4699-4706
    • Larsen, R.A.1    Chen, G.J.2    Postle, K.3
  • 40
    • 0038385104 scopus 로고    scopus 로고
    • In vivo evidence of TonB shuttling between the cytoplasmic and outer membrane in Escherichia coli
    • Larsen, R.A., Letain, T.E. Postle, K. (2003b) 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
  • 41
    • 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., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J.P. 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
  • 42
    • 33846948630 scopus 로고    scopus 로고
    • Evidence of ball-and-chain transport of ferric enterobactin through FepA
    • Ma, L., Kaserer, W., Annamalai, R., Scott, D.C., Jin, B., Jiang, X., et al. (2007) Evidence of ball-and-chain transport of ferric enterobactin through FepA. J Biol Chem 282 : 397 406.
    • (2007) J Biol Chem , vol.282 , pp. 397-406
    • Ma, L.1    Kaserer, W.2    Annamalai, R.3    Scott, D.C.4    Jin, B.5    Jiang, X.6
  • 43
    • 0025049224 scopus 로고
    • Import-defective colicin B derivatives mutated in the TonB box
    • Mende, J. Braun, V. (1990) Import-defective colicin B derivatives mutated in the TonB box. Mol Microbiol 4 : 1523 1533.
    • (1990) Mol Microbiol , vol.4 , pp. 1523-1533
    • Mende, J.1    Braun, V.2
  • 44
    • 0034093293 scopus 로고    scopus 로고
    • Substrate-induced exposure of an energy-coupling motif of a membrane transporter
    • Merianos, H.J., Lin, C.H., Kadner, R.J. Cafiso, D.S. (2000) Substrate-induced exposure of an energy-coupling motif of a membrane transporter. Nat Struct Biol 7 : 205 209.
    • (2000) Nat Struct Biol , vol.7 , pp. 205-209
    • Merianos, H.J.1    Lin, C.H.2    Kadner, R.J.3    Cafiso, D.S.4
  • 45
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press.
    • Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY : Cold Spring Harbor Laboratory Press.
    • (1972) Experiments in Molecular Genetics.
    • Miller, J.H.1
  • 46
    • 0037337264 scopus 로고    scopus 로고
    • Interactions between the outer membrane ferric citrate transporter FecA and TonB: Studies of the FecA TonB box
    • Ogierman, M. Braun, V. (2003) Interactions between the outer membrane ferric citrate transporter FecA and TonB: studies of the FecA TonB box. J Bacteriol 185 : 1870 1885.
    • (2003) J Bacteriol , vol.185 , pp. 1870-1885
    • Ogierman, M.1    Braun, V.2
  • 49
    • 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, R.M. (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
  • 50
    • 11844269327 scopus 로고    scopus 로고
    • The solution structure of the C-terminal domain of TonB and interaction studies with TonB box peptides
    • Sean Peacock, R., Weljie, A.M., Peter Howard, S., Price, F.D. Vogel, H.J. (2005) The solution structure of the C-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
    • Sean Peacock, R.1    Weljie, A.M.2    Peter Howard, S.3    Price, F.D.4    Vogel, H.J.5
  • 51
    • 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., Ozkan, E., Gardner, K.H. Deisenhofer, J. (2001) 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 USA 98 : 10676 10681.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10676-10681
    • Usher, K.C.1    Ozkan, E.2    Gardner, K.H.3    Deisenhofer, J.4
  • 53
    • 0036778139 scopus 로고    scopus 로고
    • FepA with globular domain deletions lacks activity
    • Vakharia, H.L. Postle, K. (2002) FepA with globular domain deletions lacks activity. J Bacteriol 184 : 5508 5512.
    • (2002) J Bacteriol , vol.184 , pp. 5508-5512
    • Vakharia, H.L.1    Postle, K.2
  • 54
    • 33748509727 scopus 로고    scopus 로고
    • Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance
    • Xu, Q., Ellena, J.F., Kim, M. Cafiso, D.S. (2006) Substrate-dependent unfolding of the energy coupling motif of a membrane transport protein determined by double electron-electron resonance. Biochemistry 45 : 10847 10854.
    • (2006) Biochemistry , vol.45 , pp. 10847-10854
    • Xu, Q.1    Ellena, J.F.2    Kim, M.3    Cafiso, D.S.4
  • 55
    • 0042508859 scopus 로고    scopus 로고
    • Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA
    • Yue, W.W., Grizot, S. Buchanan, S.K. (2003) Structural evidence for iron-free citrate and ferric citrate binding to the TonB-dependent outer membrane transporter FecA. J Mol Biol 332 : 353 368.
    • (2003) J Mol Biol , vol.332 , pp. 353-368
    • Yue, W.W.1    Grizot, S.2    Buchanan, S.K.3
  • 56
    • 10044257908 scopus 로고    scopus 로고
    • Colicin occlusion of OmpF and TolC channels: Outer membrane translocons for colicin import
    • Zakharov, S.D., Eroukova, V.Y., Rokitskaya, T.I., Zhalnina, M.V., Sharma, O., Loll, P.J., et al. (2004) Colicin occlusion of OmpF and TolC channels: outer membrane translocons for colicin import. Biophys J 87 : 3901 3911.
    • (2004) Biophys J , vol.87 , pp. 3901-3911
    • Zakharov, S.D.1    Eroukova, V.Y.2    Rokitskaya, T.I.3    Zhalnina, M.V.4    Sharma, O.5    Loll, P.J.6


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