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Volumn 332, Issue 5, 2003, Pages 999-1014

The Escherichia coli outer membrane cobalamin transporter BtuB: Structural analysis of calcium and substrate binding, and identification of orthologous transporters by sequence/structure conservation

Author keywords

BtuB; Calcium binding; Cobalamin; Outer membrane transport; Vitamin B12

Indexed keywords

CALCIUM; CARRIER PROTEIN; COBALAMIN; CYANOCOBALAMIN; PROTEIN BTUB; UNCLASSIFIED DRUG;

EID: 0041384402     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.07.005     Document Type: Article
Times cited : (74)

References (44)
  • 1
    • 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
    • Lundrigan M.D., Kadner R.J. 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
  • 2
    • 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. 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
  • 3
    • 0025572764 scopus 로고
    • 12 transport in Escherichia coli: Energy coupling between membranes
    • 12 transport in Escherichia coli: energy coupling between membranes. Mol. Microbiol. 4:1990;2027-2033.
    • (1990) Mol. Microbiol. , vol.4 , pp. 2027-2033
    • Kadner, R.J.1
  • 4
    • 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. 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
  • 5
    • 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. 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
  • 8
    • 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. Substrate induced transmembrane signaling in the cobalamin transporter BtuB. Nature Struct. Biol. 10:2003;394-401.
    • (2003) Nature Struct. Biol. , vol.10 , pp. 394-401
    • Chimento, D.P.1    Mohanty, A.K.2    Kadner, R.J.3    Wiener, M.C.4
  • 10
    • 0021893059 scopus 로고
    • 12 in Escherichia coli: Cloning of the btuCD region
    • 12 in Escherichia coli: cloning of the btuCD region. J. Bacteriol. 162:1985;888-896.
    • (1985) J. Bacteriol. , vol.162 , pp. 888-896
    • DeVeaux, L.C.1    Kadner, R.J.2
  • 11
    • 0037052565 scopus 로고    scopus 로고
    • The E. coli BtuCD structure: A framework for ABC transporter architecture and mechanism
    • Locher K.P., Lee A.T., Rees D.C. The E. coli BtuCD structure: a framework for ABC transporter architecture and mechanism. Science. 296:2002;1091-1098.
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 13
    • 49149124735 scopus 로고
    • Structure of thermolysin
    • Matthews B.W. Structure of thermolysin. Nature New Biol. 238:1972;41-43.
    • (1972) Nature New Biol. , vol.238 , pp. 41-43
    • Matthews, B.W.1
  • 14
    • 0021112767 scopus 로고
    • Divalent cation sites in tomato bushy stunt virus. Difference maps at 2. 9 Å resolution
    • Hogle J., Kirchhausen T., Harrison S.C. Divalent cation sites in tomato bushy stunt virus. Difference maps at 2.9 Å resolution. J. Mol. Biol. 171:1983;95-100.
    • (1983) J. Mol. Biol. , vol.171 , pp. 95-100
    • Hogle, J.1    Kirchhausen, T.2    Harrison, S.C.3
  • 17
    • 0030933176 scopus 로고    scopus 로고
    • A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-δ1
    • Essen L.O., Perisic O., Lynch D.E., Katan M., Williams R.L. A ternary metal binding site in the C2 domain of phosphoinositide-specific phospholipase C-δ1. Biochemistry. 36:1997;2753-2762.
    • (1997) Biochemistry , vol.36 , pp. 2753-2762
    • Essen, L.O.1    Perisic, O.2    Lynch, D.E.3    Katan, M.4    Williams, R.L.5
  • 18
    • 0033179802 scopus 로고    scopus 로고
    • The geometry of metal-protein interactions relevant to proteins
    • Harding M.M. The geometry of metal-protein interactions relevant to proteins. Acta Crystallog. sect. D. 55:1999;1432-1433.
    • (1999) Acta Crystallog. sect. D , vol.55 , pp. 1432-1433
    • Harding, M.M.1
  • 19
    • 0033937430 scopus 로고    scopus 로고
    • The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions
    • Harding M.M. The geometry of metal-ligand interactions relevant to proteins. II. Angles at the metal atom, additional weak metal-donor interactions. Acta Crystallog. sect. D. 56:2000;857-867.
    • (2000) Acta Crystallog. sect. D , vol.56 , pp. 857-867
    • Harding, M.M.1
  • 21
    • 0036219377 scopus 로고    scopus 로고
    • The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer
    • Sintchak M.D., Arjara G., Kellogg B.A., Stubbe J., Drennan C.L. The crystal structure of class II ribonucleotide reductase reveals how an allosterically regulated monomer mimics a dimer. Nature Struct. Biol. 9:2002;293-300.
    • (2002) Nature Struct. Biol. , vol.9 , pp. 293-300
    • Sintchak, M.D.1    Arjara, G.2    Kellogg, B.A.3    Stubbe, J.4    Drennan, C.L.5
  • 24
    • 0037168666 scopus 로고    scopus 로고
    • The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter
    • Borths E.L., Locher K.P., Lee A.T., Rees D.C. The structure of Escherichia coli BtuF and binding to its cognate ATP binding cassette transporter. Proc. Natl Acad. Sci. USA. 99:2002;16642-16647.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 16642-16647
    • Borths, E.L.1    Locher, K.P.2    Lee, A.T.3    Rees, D.C.4
  • 25
    • 0037424465 scopus 로고    scopus 로고
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding
    • 12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 278:2003;8429-8434.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8429-8434
    • Karpowich, N.K.1    Huang, H.H.2    Smith, P.C.3    Hunt, J.F.4
  • 26
    • 0018200003 scopus 로고
    • 12 in Escherichia coli. Corrinoid specificity of the outer membrane receptor
    • 12 in Escherichia coli. Corrinoid specificity of the outer membrane receptor. J. Biol. Chem. 253:1978;1341-1346.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1341-1346
    • Kenley, J.S.1    Leighton, M.2    Bradbeer, C.3
  • 27
    • 0023000315 scopus 로고
    • A requirement for calcium in the transport of cobalamin across the outer membrane of Escherichia coli
    • Bradbeer C., Reynolds P.R., Bauler G.M., Fernandez M.T. A requirement for calcium in the transport of cobalamin across the outer membrane of Escherichia coli. J. Biol. Chem. 261:1986;2520-2523.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2520-2523
    • Bradbeer, C.1    Reynolds, P.R.2    Bauler, G.M.3    Fernandez, M.T.4
  • 28
    • 0030925485 scopus 로고    scopus 로고
    • Surface signaling: Novel transcription initiation mechanism starting from the cell surface
    • Braun V. 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
  • 29
    • 0015506348 scopus 로고
    • The structure of thermolysin: An electron density map at 2.3 Å resolution
    • Colman P.M., Jansonius J.N., Matthews B.W. The structure of thermolysin: an electron density map at 2.3 Å resolution. J. Mol. Biol. 70:1972;701-724.
    • (1972) J. Mol. Biol. , vol.70 , pp. 701-724
    • Colman, P.M.1    Jansonius, J.N.2    Matthews, B.W.3
  • 30
    • 0029924329 scopus 로고    scopus 로고
    • Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta
    • Essen L.O., Perisic O., Cheung R., Katan M., Williams R.L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta. Nature. 380:1996;595-602.
    • (1996) Nature , vol.380 , pp. 595-602
    • Essen, L.O.1    Perisic, O.2    Cheung, R.3    Katan, M.4    Williams, R.L.5
  • 31
    • 0025121127 scopus 로고
    • Interdependence of calcium and cobalamin binding by wild-type and mutant BtuB protein in the outer membrane of Escherichia coli
    • Bradbeer C., Gudmundsdottir A. Interdependence of calcium and cobalamin binding by wild-type and mutant BtuB protein in the outer membrane of Escherichia coli. J. Bacteriol. 172:1990;4919-4926.
    • (1990) J. Bacteriol. , vol.172 , pp. 4919-4926
    • Bradbeer, C.1    Gudmundsdottir, A.2
  • 33
    • 0020475829 scopus 로고
    • Divalent ion-dependent reversible swelling of tomato bushy stunt virus and organization of the expanded virion
    • Kruse J., Kruse K.M., Witz J. Divalent ion-dependent reversible swelling of tomato bushy stunt virus and organization of the expanded virion. J. Mol. Biol. 162:1982;393-417.
    • (1982) J. Mol. Biol. , vol.162 , pp. 393-417
    • Kruse, J.1    Kruse, K.M.2    Witz, J.3
  • 34
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: Structural and functional diversity
    • Nalefski E.A., Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 5:1996;2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 36
    • 0032431907 scopus 로고    scopus 로고
    • Coupled changes in translation and transcription during cobalamin-dependent regulation of btuB expression in Escherichia coli
    • Nou X., Kadner R.J. Coupled changes in translation and transcription during cobalamin-dependent regulation of btuB expression in Escherichia coli. J. Bacteriol. 180:1998;6719-6728.
    • (1998) J. Bacteriol. , vol.180 , pp. 6719-6728
    • Nou, X.1    Kadner, R.J.2
  • 37
    • 0028922586 scopus 로고
    • LIGPLOT: A program to generate schematic diagrams of protein-ligand interactions
    • Wallace A.C., Laskowski R.A., Thornton J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8:1995;127-134.
    • (1995) Protein Eng. , vol.8 , pp. 127-134
    • Wallace, A.C.1    Laskowski, R.A.2    Thornton, J.M.3
  • 40
    • 0032127358 scopus 로고    scopus 로고
    • The Biology Workbench-a seamless database and analysis environment for the biologist
    • Subramaniam S. The Biology Workbench-a seamless database and analysis environment for the biologist. Proteins: Struct. Funct. Genet. 32:1998;1-2.
    • (1998) Proteins: Struct. Funct. Genet. , vol.32 , pp. 1-2
    • Subramaniam, S.1
  • 41
    • 0033990087 scopus 로고    scopus 로고
    • The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment
    • Aiyar A. The use of CLUSTAL W and CLUSTAL X for multiple sequence alignment. Methods Mol. Biol. 132:2000;221-241.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 221-241
    • Aiyar, A.1
  • 42
    • 0002051540 scopus 로고    scopus 로고
    • BioEdit: A user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT
    • Hall T.A. BioEdit: a user-friendly biological sequence alignment editor and analysis program for Windows 95/98/NT. Nucl. Acids Symp. Series. 41:1999;95-98.
    • (1999) Nucl. Acids Symp. Series , vol.41 , pp. 95-98
    • Hall, T.A.1
  • 43
    • 0028348081 scopus 로고
    • Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis
    • Murzin A.G., Lesk A.M., Chothia C. Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis. J. Mol. Biol. 236:1994;1369-1381.
    • (1994) J. Mol. Biol. , vol.236 , pp. 1369-1381
    • Murzin, A.G.1    Lesk, A.M.2    Chothia, C.3
  • 44
    • 0032579317 scopus 로고    scopus 로고
    • Shear numbers of protein beta-barrels: Definition refinements and statistics
    • Liu W.M. Shear numbers of protein beta-barrels: definition refinements and statistics. J. Mol. Biol. 275:1998;541-545.
    • (1998) J. Mol. Biol. , vol.275 , pp. 541-545
    • Liu, W.M.1


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