메뉴 건너뛰기




Volumn 53, Issue 12, 2014, Pages 2017-2031

Crystal and solution structure analysis of FhuD2 from Staphylococcus aureus in multiple Unliganded conformations and bound to ferrioxamine-B

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; ESCHERICHIA COLI; HYDROGEN BONDS; LIGANDS; PLANTS (BOTANY); PROTEINS;

EID: 84898063576     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401349d     Document Type: Article
Times cited : (31)

References (45)
  • 1
    • 0346749526 scopus 로고    scopus 로고
    • The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport
    • Sebulsky, M. T., Shilton, B. H., Speziali, C. D., and Heinrichs, D. E. (2003) The role of FhuD2 in iron(III)-hydroxamate transport in Staphylococcus aureus. Demonstration that FhuD2 binds iron(III)-hydroxamates but with minimal conformational change and implication of mutations on transport J. Biol. Chem. 278, 49890-49900
    • (2003) J. Biol. Chem. , vol.278 , pp. 49890-49900
    • Sebulsky, M.T.1    Shilton, B.H.2    Speziali, C.D.3    Heinrichs, D.E.4
  • 2
    • 11144235166 scopus 로고    scopus 로고
    • FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: A case of gene duplication and lateral transfer
    • Sebulsky, M. T., Speziali, C. D., Shilton, B. H., Edgell, D. R., and Heinrichs, D. E. (2004) FhuD1, a ferric hydroxamate-binding lipoprotein in Staphylococcus aureus: A case of gene duplication and lateral transfer J. Biol. Chem. 279, 53152-53159
    • (2004) J. Biol. Chem. , vol.279 , pp. 53152-53159
    • Sebulsky, M.T.1    Speziali, C.D.2    Shilton, B.H.3    Edgell, D.R.4    Heinrichs, D.E.5
  • 5
    • 0029981539 scopus 로고    scopus 로고
    • Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes
    • Quiocho, F. A. and Ledvina, P. S. (1996) Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: Variation of common themes Mol. Microbiol. 20, 17-25
    • (1996) Mol. Microbiol. , vol.20 , pp. 17-25
    • Quiocho, F.A.1    Ledvina, P.S.2
  • 6
    • 0024726144 scopus 로고
    • Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport
    • Bishop, L., Agbayani, R., Ambudkar, S. V., Maloney, P. C., and Ames, G. F. (1989) Reconstitution of a bacterial periplasmic permease in proteoliposomes and demonstration of ATP hydrolysis concomitant with transport Proc. Natl. Acad. Sci. U.S.A. 86, 6953-6957
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 6953-6957
    • Bishop, L.1    Agbayani, R.2    Ambudkar, S.V.3    Maloney, P.C.4    Ames, G.F.5
  • 7
    • 0026549522 scopus 로고
    • Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins
    • Davidson, A., Shuman, H., and Nikaido, H. (1992) Mechanism of maltose transport in Escherichia coli: Transmembrane signaling by periplasmic binding proteins Proc. Natl. Acad. Sci. U.S.A. 89, 2360-2364
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 2360-2364
    • Davidson, A.1    Shuman, H.2    Nikaido, H.3
  • 10
    • 0034127329 scopus 로고    scopus 로고
    • The structure of the ferric siderophore binding protein FhuD complexed with gallichrome
    • Clarke, T. E., Ku, S. Y., Dougan, D. R., Vogel, H. J., and Tari, L. W. (2000) The structure of the ferric siderophore binding protein FhuD complexed with gallichrome Nat. Struct. Biol. 7, 287-291
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 287-291
    • Clarke, T.E.1    Ku, S.Y.2    Dougan, D.R.3    Vogel, H.J.4    Tari, L.W.5
  • 11
    • 0031053054 scopus 로고    scopus 로고
    • Reductive alkylation of lysine residues to alter crystallization properties of proteins
    • Rayment, I. (1997) Reductive alkylation of lysine residues to alter crystallization properties of proteins Methods Enzymol. 276, 171-179
    • (1997) Methods Enzymol. , vol.276 , pp. 171-179
    • Rayment, I.1
  • 12
    • 0041333138 scopus 로고    scopus 로고
    • Enhancing Protein Crystallization through Precipitant Synergy
    • Majeed, S., Ofek, G., Belachew, A., Huang, C., Zhou, T., and Kwong, P. (2003) Enhancing Protein Crystallization through Precipitant Synergy Structure 11, 1061-1070
    • (2003) Structure , vol.11 , pp. 1061-1070
    • Majeed, S.1    Ofek, G.2    Belachew, A.3    Huang, C.4    Zhou, T.5    Kwong, P.6
  • 13
    • 1842555070 scopus 로고    scopus 로고
    • Rational protein crystallization by mutational surface engineering
    • Derewenda, Z. S. (2004) Rational protein crystallization by mutational surface engineering Structure 12, 529-535
    • (2004) Structure , vol.12 , pp. 529-535
    • Derewenda, Z.S.1
  • 15
    • 50249136103 scopus 로고    scopus 로고
    • Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7
    • Langer, G., Cohen, S. X., Lamzin, V. S., and Perrakis, A. (2008) Automated macromolecular model building for X-ray crystallography using ARP/wARP version 7 Nat. Protoc. 3, 1171-1179
    • (2008) Nat. Protoc. , vol.3 , pp. 1171-1179
    • Langer, G.1    Cohen, S.X.2    Lamzin, V.S.3    Perrakis, A.4
  • 17
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme
    • Hayward, S. and Berendsen, H. J. (1998) Systematic analysis of domain motions in proteins from conformational change: New results on citrate synthase and T4 lysozyme Proteins 30, 144-154
    • (1998) Proteins , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.2
  • 20
    • 0002526583 scopus 로고
    • Complexation of Iron by Siderophores: A Review of Their Solution and Structural Chemistry and Biological Function
    • Springer, Berlin
    • Raymond, K., Müller, G., and Matzanke, B. (1984) Complexation of Iron by Siderophores: A Review of Their Solution and Structural Chemistry and Biological Function. In Topics in Current Chemistry, pp 49-102, Springer, Berlin.
    • (1984) Topics in Current Chemistry , pp. 49-102
    • Raymond, K.1    Muller, G.2    Matzanke, B.3
  • 21
    • 0035161308 scopus 로고    scopus 로고
    • Crystal structure of ferrioxamine B: A comparative analysis and implications for molecular recognition
    • Dhungana, S., White, P. S., and Crumbliss, A. L. (2001) Crystal structure of ferrioxamine B: A comparative analysis and implications for molecular recognition JBIC, J. Biol. Inorg. Chem. 6, 810-818
    • (2001) JBIC, J. Biol. Inorg. Chem. , vol.6 , pp. 810-818
    • Dhungana, S.1    White, P.S.2    Crumbliss, A.L.3
  • 22
    • 0026244044 scopus 로고
    • GNOM: A program package for small-angle scattering data processing
    • Semenyuk, A. and Svergun, D. (1991) GNOM: A program package for small-angle scattering data processing J. Appl. Crystallogr. 24, 537-540
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 537-540
    • Semenyuk, A.1    Svergun, D.2
  • 24
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo, R. P. and Tainer, J. A. (2011) Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law Biopolymers 95, 559-571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 25
    • 84876800465 scopus 로고    scopus 로고
    • Accurate assessment of mass, models and resolution by small-angle scattering
    • Rambo, R. P. and Tainer, J. A. (2013) Accurate assessment of mass, models and resolution by small-angle scattering Nature 496, 477-481
    • (2013) Nature , vol.496 , pp. 477-481
    • Rambo, R.P.1    Tainer, J.A.2
  • 26
    • 77954280480 scopus 로고    scopus 로고
    • FoXS: A web server for rapid computation and fitting of SAXS profiles
    • Schneidman-Duhovny, D., Hammel, M., and Sali, A. (2010) FoXS: A web server for rapid computation and fitting of SAXS profiles Nucleic Acids Res. 38, W540-W544
    • (2010) Nucleic Acids Res. , vol.38
    • Schneidman-Duhovny, D.1    Hammel, M.2    Sali, A.3
  • 27
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2: A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A. M., Procter, J. B., Martin, D. M. A., Clamp, M., and Barton, G. J. (2009) Jalview Version 2: A multiple sequence alignment editor and analysis workbench Bioinformatics 25, 1189-1191
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.A.3    Clamp, M.4    Barton, G.J.5
  • 28
    • 3242878412 scopus 로고    scopus 로고
    • 3DCoffee@igs: A web server for combining sequences and structures into a multiple sequence alignment
    • Poirot, O., Suhre, K., Abergel, C., OToole, E., and Notredame, C. (2004) 3DCoffee@igs: A web server for combining sequences and structures into a multiple sequence alignment Nucleic Acids Res. 32, W37-W40
    • (2004) Nucleic Acids Res. , vol.32
    • Poirot, O.1    Suhre, K.2    Abergel, C.3    Otoole, E.4    Notredame, C.5
  • 30
    • 65449162362 scopus 로고    scopus 로고
    • Siderophore-mediated iron acquisition systems in Bacillus cereus: Identification of receptors for anthrax virulence-associated petrobactin
    • Zawadzka, A. M., Abergel, R. J., Nichiporuk, R., Andersen, U. N., and Raymond, K. N. (2009) Siderophore-mediated iron acquisition systems in Bacillus cereus: Identification of receptors for anthrax virulence-associated petrobactin Biochemistry 48, 3645-3657
    • (2009) Biochemistry , vol.48 , pp. 3645-3657
    • Zawadzka, A.M.1    Abergel, R.J.2    Nichiporuk, R.3    Andersen, U.N.4    Raymond, K.N.5
  • 31
    • 34548671159 scopus 로고    scopus 로고
    • Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
    • Hvorup, R. N., Goetz, B. A., Niederer, M., Hollenstein, K., Perozo, E., and Locher, K. P. (2007) Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF Science 317, 1387-1390
    • (2007) Science , vol.317 , pp. 1387-1390
    • Hvorup, R.N.1    Goetz, B.A.2    Niederer, M.3    Hollenstein, K.4    Perozo, E.5    Locher, K.P.6
  • 32
    • 50049095291 scopus 로고    scopus 로고
    • The dynamics of the MBP-MalFGK(2) interaction: A prototype for binding protein dependent ABC-transporter systems
    • Shilton, B. H. (2008) The dynamics of the MBP-MalFGK(2) interaction: A prototype for binding protein dependent ABC-transporter systems Biochim. Biophys. Acta 1778, 1772-1780
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1772-1780
    • Shilton, B.H.1
  • 33
  • 35
    • 61449341855 scopus 로고    scopus 로고
    • Structure and mechanism of ATP-binding cassette transporters
    • Locher, K. P. (2009) Structure and mechanism of ATP-binding cassette transporters Philos. Trans. R. Soc., B 364, 239-245
    • (2009) Philos. Trans. R. Soc., B , vol.364 , pp. 239-245
    • Locher, K.P.1
  • 36
    • 77949263042 scopus 로고    scopus 로고
    • A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation
    • Lewinson, O., Lee, A. T., Locher, K. P., and Rees, D. C. (2010) A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation Nat. Struct. Mol. Biol. 17, 332-338
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 332-338
    • Lewinson, O.1    Lee, A.T.2    Locher, K.P.3    Rees, D.C.4
  • 37
    • 84859264217 scopus 로고    scopus 로고
    • 12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
    • 12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF FEBS Lett. 586, 972-976
    • (2012) FEBS Lett. , vol.586 , pp. 972-976
    • Korkhov, V.M.1    Mireku, S.A.2    Hvorup, R.N.3    Locher, K.P.4
  • 39
    • 0037134502 scopus 로고    scopus 로고
    • X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin
    • Clarke, T. E., Braun, V., Winkelmann, G., Tari, L. W., and Vogel, H. J. (2002) X-ray crystallographic structures of the Escherichia coli periplasmic protein FhuD bound to hydroxamate-type siderophores and the antibiotic albomycin J. Biol. Chem. 277, 13966-13972
    • (2002) J. Biol. Chem. , vol.277 , pp. 13966-13972
    • Clarke, T.E.1    Braun, V.2    Winkelmann, G.3    Tari, L.W.4    Vogel, H.J.5
  • 40
    • 51349104365 scopus 로고    scopus 로고
    • Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter
    • Orelle, C., Ayvaz, T., Everly, R. M., Klug, C. S., and Davidson, A. L. (2008) Both maltose-binding protein and ATP are required for nucleotide-binding domain closure in the intact maltose ABC transporter Proc. Natl. Acad. Sci. U.S.A. 105, 12837-12842
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 12837-12842
    • Orelle, C.1    Ayvaz, T.2    Everly, R.M.3    Klug, C.S.4    Davidson, A.L.5
  • 41
    • 79957932347 scopus 로고    scopus 로고
    • Crystal structure of the maltose transporter in a pretranslocation intermediate state
    • Oldham, M. L. and Chen, J. (2011) Crystal structure of the maltose transporter in a pretranslocation intermediate state Science 332, 1202-1205
    • (2011) Science , vol.332 , pp. 1202-1205
    • Oldham, M.L.1    Chen, J.2
  • 42
    • 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., and Chen, J. (2007) Crystal structure of a catalytic intermediate of the maltose transporter Nature 450, 515-521
    • (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
  • 43
    • 77951231340 scopus 로고    scopus 로고
    • Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate
    • Gould, A. D. and Shilton, B. H. (2010) Studies of the maltose transport system reveal a mechanism for coupling ATP hydrolysis to substrate translocation without direct recognition of substrate J. Biol. Chem. 285, 11290-11296
    • (2010) J. Biol. Chem. , vol.285 , pp. 11290-11296
    • Gould, A.D.1    Shilton, B.H.2
  • 44
    • 78650070642 scopus 로고    scopus 로고
    • Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter
    • Cui, J., Qasim, S., and Davidson, A. L. (2010) Uncoupling substrate transport from ATP hydrolysis in the Escherichia coli maltose transporter J. Biol. Chem. 285, 39986-39993
    • (2010) J. Biol. Chem. , vol.285 , pp. 39986-39993
    • Cui, J.1    Qasim, S.2    Davidson, A.L.3
  • 45
    • 84882940564 scopus 로고    scopus 로고
    • Accurate SAXS Profile Computation and its Assessment by Contrast Variation Experiments
    • Schneidman-Duhovny, D., Hammel, M., Tainer, J. A., and Sali, A. (2013) Accurate SAXS Profile Computation and its Assessment by Contrast Variation Experiments Biophys. J. 105, 962-974
    • (2013) Biophys. J. , vol.105 , pp. 962-974
    • Schneidman-Duhovny, D.1    Hammel, M.2    Tainer, J.A.3    Sali, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.