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Volumn 490, Issue 7420, 2012, Pages 367-372

Structure of AMP-PNP-bound vitamin B 12 transporter BtuCD-F

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ADENYLYLIMIDODIPHOSPHATE; CYANOCOBALAMIN; DIMER; LIPOSOME; TRANSPORTER BINDING PROTEIN COMPLEX BTUCD BTUF; UNCLASSIFIED DRUG;

EID: 84867670628     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11442     Document Type: Article
Times cited : (138)

References (44)
  • 2
    • 44949249999 scopus 로고    scopus 로고
    • Structure, function, and evolution of bacterial ATP-binding cassette systems
    • Davidson, A. L., Dassa, E., Orelle, C. & Chen, J. Structure, function, and evolution of bacterial ATP-binding cassette systems. Microbiol. Mol. Biol. Rev. 72, 317-364 (2008).
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 317-364
    • Davidson, A.L.1    Dassa, E.2    Orelle, C.3    Chen, J.4
  • 5
    • 79960053262 scopus 로고    scopus 로고
    • The structural basis of modularity inECF-type ABC transporters
    • Erkens, G. B. et al. The structural basis of modularity inECF-type ABC transporters. Nature Struct. Mol. Biol. 18, 755-760 (2011).
    • (2011) Nature Struct. Mol. Biol. , vol.18 , pp. 755-760
    • Erkens, G.B.1
  • 6
    • 0019230249 scopus 로고
    • Transportofvitamin B12 inEscherichia coli. Some observationsonthe rolesofthe gene productsofBtuC and TonB
    • Reynolds, P. R., Mottur, G. P. & Bradbeer, C. Transportofvitamin B12 inEscherichia coli. Some observationsonthe rolesofthe gene productsofBtuC and TonB. J. Biol. Chem. 255, 4313-4319 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 4313-4319
    • Reynolds, P.R.1    Mottur, G.P.2    Bradbeer, C.3
  • 7
    • 0021893059 scopus 로고
    • Transport of vitamin B12 in Escherichia coli: Cloning of the btuCD region
    • DeVeaux, L. C. & Kadner, R. J. Transport of vitamin B12 in Escherichia coli: cloning of the btuCD region. J. Bacteriol. 162, 888-896 (1985).
    • (1985) J. Bacteriol. , vol.162 , pp. 888-896
    • Deveaux, L.C.1    Kadner, R.J.2
  • 8
    • 0032811904 scopus 로고    scopus 로고
    • Identification and molecular characterization of a novel Salmonella enteritidis pathogenicity islet encoding an ABC transporter
    • Pattery, T., Hernalsteens, J. P. & De Greve, H. Identification and molecular characterization of a novel Salmonella enteritidis pathogenicity islet encoding an ABC transporter. Mol. Microbiol. 33, 791-805 (1999).
    • (1999) Mol. Microbiol. , vol.33 , pp. 791-805
    • Pattery, T.1    Hernalsteens, J.P.2    De Greve, H.3
  • 9
    • 0034011567 scopus 로고    scopus 로고
    • The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium
    • Janakiraman, A. & Slauch, J. M. The putative iron transport system SitABCD encoded on SPI1 is required for full virulence of Salmonella typhimurium. Mol. Microbiol. 35, 1146-1155 (2000).
    • (2000) Mol. Microbiol. , vol.35 , pp. 1146-1155
    • Janakiraman, A.1    Slauch, J.M.2
  • 10
    • 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, 1091-1098 (2002).
    • (2002) Science , vol.296 , pp. 1091-1098
    • Locher, K.P.1    Lee, A.T.2    Rees, D.C.3
  • 11
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup, R. N. et al. Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF. Science 317, 1387-1390 (2007)
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1
  • 12
    • 84859264217 scopus 로고    scopus 로고
    • Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
    • Korkhov, V. M., Mireku, S. A., Hvorup, R. N. & Locher, K. P. Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF. FEBS Lett. 586, 972-976 (2012).
    • (2012) FEBS Lett. , vol.586 , pp. 972-976
    • Korkhov, V.M.1    Mireku, S.A.2    Hvorup, R.N.3    Locher, K.P.4
  • 13
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J. & Locher, K. P. Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185 (2006).
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 14
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility inthe ABC transporter MsbA:alternating accesswithatwist
    • Ward, A., Reyes, C. L., Yu, J., Roth, C. B. & Chang, G. Flexibility inthe ABC transporter MsbA:alternating accesswithatwist. Proc. Natl Acad. Sci. USA104, 19005-19010 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 15
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham, M. L., Khare, D., Quiocho, F. A., Davidson, A. L. & Chen, J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 450, 515-521 (2007).
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 16
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • Oldham, M. L. & Chen, J. Crystal structure of the maltose transporter in a pretranslocation intermediate state. Science 332, 1202-1205 (2011).
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 18
    • 77949263042 scopus 로고    scopus 로고
    • Adistinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation
    • Lewinson, O., Lee, A. T., Locher, K. P. & Rees, D. C. Adistinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation. Nature Struct. Mol. Biol. 17, 332-338 (2010).
    • (2010) Nature Struct. Mol. Biol. , vol.17 , pp. 332-338
    • Lewinson, O.1    Lee, A.T.2    Locher, K.P.3    Rees, D.C.4
  • 19
    • 80455163144 scopus 로고    scopus 로고
    • Bacterial ATP-driven transporters of transition metals: Physiological roles, mechanisms of action, and roles in bacterial virulence
    • Klein, J. S. & Lewinson, O. Bacterial ATP-driven transporters of transition metals: physiological roles, mechanisms of action, and roles in bacterial virulence. Metallomics 3, 1098-1108 (2011).
    • (2011) Metallomics , vol.3 , pp. 1098-1108
    • Klein, J.S.1    Lewinson, O.2
  • 20
    • 33846601303 scopus 로고    scopus 로고
    • An inward-facing conformation of a putative metal-chelate-type ABC transporter
    • Pinkett, H. W., Lee, A. T., Lum, P., Locher, K. P. & Rees, D. C. An inward-facing conformation of a putative metal-chelate-type ABC transporter. Science 315, 373-377 (2007).
    • (2007) Science , vol.315 , pp. 373-377
    • Pinkett, H.W.1    Lee, A.T.2    Lum, P.3    Locher, K.P.4    Rees, D.C.5
  • 21
    • 0036342413 scopus 로고    scopus 로고
    • ATP bindingtothe motor domain fromanABC transporter drives formation of a nucleotide sandwich dimer
    • Smith, P. C. et al. ATP bindingtothe motor domain fromanABC transporter drives formation of a nucleotide sandwich dimer. Mol. Cell 10, 139-149 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 139-149
    • Smith, P.C.1
  • 22
    • 21244454073 scopus 로고    scopus 로고
    • H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB
    • Zaitseva, J., Jenewein, S., Jumpertz, T., Holland, I. B. & Schmitt, L. H662 is the linchpin of ATP hydrolysis in the nucleotide-binding domain of the ABC transporter HlyB. EMBO J. 24, 1901-1910 (2005).
    • (2005) EMBO J. , vol.24 , pp. 1901-1910
    • Zaitseva, J.1    Jenewein, S.2    Jumpertz, T.3    Holland, I.B.4    Schmitt, L.5
  • 23
    • 33749076230 scopus 로고    scopus 로고
    • Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter
    • Procko, E., Ferrin-O'Connell, I., Ng, S. L. & Gaudet, R. Distinct structural and functional properties of the ATPase sites in an asymmetric ABC transporter. Mol. Cell 24, 51-62 (2006).
    • (2006) Mol. Cell , vol.24 , pp. 51-62
    • Procko, E.1    Ferrin-O'Connell, I.2    Ng, S.L.3    Gaudet, R.4
  • 24
    • 33847134349 scopus 로고    scopus 로고
    • Structureof the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson, R. J. & Locher, K. P. Structureof the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 581, 935-938 (2007).
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 25
    • 69949136235 scopus 로고    scopus 로고
    • Insights into how nucleotide-binding domains power ABC transport
    • Newstead, S. et al. Insights into how nucleotide-binding domains power ABC transport. Structure 17, 1213-1222 (2009).
    • (2009) Structure , vol.17 , pp. 1213-1222
    • Newstead, S.1
  • 26
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner, K. P. et al. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101, 789-800 (2000).
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1
  • 27
    • 34548529916 scopus 로고    scopus 로고
    • Crystal structure of a thermally stable rhodopsin mutant
    • Standfuss, J. et al. Crystal structure of a thermally stable rhodopsin mutant. J. Mol. Biol. 372, 1179-1188 (2007).
    • (2007) J. Mol. Biol. , vol.372 , pp. 1179-1188
    • Standfuss, J.1
  • 28
    • 72449164409 scopus 로고    scopus 로고
    • Transport mechanismofabacterial homologue of glutamate transporters
    • Reyes, N., Ginter, C. & Boudker, O. Transport mechanismofabacterial homologue of glutamate transporters. Nature 462, 880-885 (2009).
    • (2009) Nature , vol.462 , pp. 880-885
    • Reyes, N.1    Ginter, C.2    Boudker, O.3
  • 29
    • 34447311648 scopus 로고    scopus 로고
    • Uptake or extrusion: Crystal structures of full ABC transporters suggest a common mechanism
    • Dawson, R. J., Hollenstein, K. & Locher, K. P. Uptake or extrusion: crystal structures of full ABC transporters suggest a common mechanism. Mol. Microbiol. 65, 250-257 (2007).
    • (2007) Mol. Microbiol. , vol.65 , pp. 250-257
    • Dawson, R.J.1    Hollenstein, K.2    Locher, K.P.3
  • 30
    • 58149512047 scopus 로고    scopus 로고
    • Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking
    • Goetz, B. A., Perozo, E. & Locher, K. P. Distinct gate conformations of the ABC transporter BtuCD revealed by electron spin resonance spectroscopy and chemical cross-linking. FEBS Lett. 583, 266-270 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 266-270
    • Goetz, B.A.1    Perozo, E.2    Locher, K.P.3
  • 31
    • 81755171418 scopus 로고    scopus 로고
    • Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle
    • Joseph, B., Jeschke, G., Goetz, B. A., Locher, K. P. & Bordignon, E. Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle. J. Biol. Chem. 286, 41008-41017 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 41008-41017
    • Joseph, B.1    Jeschke, G.2    Goetz, B.A.3    Locher, K.P.4    Bordignon, E.5
  • 32
    • 0030925920 scopus 로고    scopus 로고
    • Pfam: A comprehensive database of protein domain families based on seed alignments
    • Sonnhammer, E. L., Eddy, S. R. & Durbin, R. Pfam: a comprehensive database of protein domain families based on seed alignments. Proteins 28, 405-420 (1997).
    • (1997) Proteins , vol.28 , pp. 405-420
    • Sonnhammer, E.L.1    Eddy, S.R.2    Durbin, R.3
  • 33
    • 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, 16642-16647 (2002).
    • (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
  • 34
    • 0037424465 scopus 로고    scopus 로고
    • Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding
    • Karpowich, N. K., Huang, H. H., Smith, P. C. & Hunt, J. F. Crystal structures of the BtuF periplasmic-binding protein for vitamin B12 suggest a functionally important reduction in protein mobility upon ligand binding. J. Biol. Chem. 278, 8429-8434 (2003).
    • (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
  • 35
    • 0014029736 scopus 로고
    • Simpleallosteric model for membrane pumps
    • Jardetzky, O. Simpleallosteric model for membrane pumps. Nature 211, 969-970 (1966).
    • (1966) Nature , vol.211 , pp. 969-970
    • Jardetzky, O.1
  • 36
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporterincomplex with its binding protein
    • Hollenstein, K., Frei, D. C. & Locher, K. P. Structure of an ABC transporterincomplex with its binding protein. Nature 446, 213-216 (2007)
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 37
    • 61449341855 scopus 로고    scopus 로고
    • Review. Structure and mechanism of ATP-binding cassette transporters
    • Locher, K. P. Review. Structure and mechanism of ATP-binding cassette transporters. Phil. Trans. R. Soc. Lond. B 364, 239-245 (2009).
    • (2009) Phil. Trans. R. Soc. Lond. B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 38
    • 0041529863 scopus 로고    scopus 로고
    • The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA
    • Patzlaff, J. S., van der Heide, T. & Poolman, B. The ATP/substrate stoichiometry of the ATP-binding cassette (ABC) transporter OpuA. J. Biol. Chem. 278, 29546-29551 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 29546-29551
    • Patzlaff, J.S.1    Van Der Heide, T.2    Poolman, B.3
  • 39
    • 0023874147 scopus 로고
    • A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: Application to lens ATPases
    • Chifflet, S., Torriglia, A., Chiesa, R. & Tolosa, S. A method for the determination of inorganic phosphate in the presence of labile organic phosphate and high concentrations of protein: application to lens ATPases. Anal. Biochem. 168, 1-4 (1988).
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 42
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 43
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes: Crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis
    • Strong, M. et al. Toward the structural genomics of complexes: crystal structure of a PE/PPE protein complex from Mycobacterium tuberculosis. Proc. Natl Acad. Sci. USA 103, 8060-8065 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 8060-8065
    • Strong, M.1
  • 44
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • Dundas, J. et al. CASTp: computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues. Nucleic Acids Res. 34, W116-W118 (2006).
    • (2006) Nucleic Acids Res. , vol.34
    • Dundas, J.1


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