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Volumn 17, Issue 7, 2009, Pages 1024-1033

Formation of the Complex between DsbD and PilB N-Terminal Domains from Neisseria meningitidis Necessitates an Adaptability of nDsbD

Author keywords

MICROBIO; PROTEINS

Indexed keywords

AMIDE; BACTERIAL PROTEIN; DISULFIDE; MEMBRANE PROTEIN; PILB PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 67649980041     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2009.05.011     Document Type: Article
Times cited : (7)

References (29)
  • 2
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr D.D., Dyson H.J., and Wright P.E. An NMR perspective on enzyme dynamics. Chem. Rev. 106 (2006) 3055-3079
    • (2006) Chem. Rev. , vol.106 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 3
    • 40849102348 scopus 로고    scopus 로고
    • 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1
    • 15N relaxation analysis of the free and bound states of the ubiquitin-like domain of human plexin-B1 and the small GTPase Rac1. J. Mol. Biol. 377 (2008) 1474-1487
    • (2008) J. Mol. Biol. , vol.377 , pp. 1474-1487
    • Bouguet-Bonnet, S.1    Buck, M.2
  • 4
    • 33845945906 scopus 로고    scopus 로고
    • The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases
    • Brot N., Collet J.F., Johnson L.C., Jönsson T.J., Weissbach H., and Lowther W.T. The thioredoxin domain of Neisseria gonorrhoeae PilB can use electrons from DsbD to reduce downstream methionine sulfoxide reductases. J. Biol. Chem. 281 (2006) 32668-32675
    • (2006) J. Biol. Chem. , vol.281 , pp. 32668-32675
    • Brot, N.1    Collet, J.F.2    Johnson, L.C.3    Jönsson, T.J.4    Weissbach, H.5    Lowther, W.T.6
  • 5
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR System
    • Brunger A.T. Version 1.2 of the Crystallography and NMR System. Nat. Protoc. 2 (2007) 2728-2733
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 6
    • 0034011364 scopus 로고    scopus 로고
    • Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm
    • Chung J., Chen T., and Missiakas D. Transfer of electrons across the cytoplasmic membrane by DsbD, a membrane protein involved in thiol-disulphide exchange and protein folding in the bacterial periplasm. Mol. Microbiol. 35 (2000) 1099-1109
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 8
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: a protein-protein docking approach based on biochemical and/or biophysical information
    • Dominguez C., Boelens R., and Bonvin A.M.J.J. HADDOCK: a protein-protein docking approach based on biochemical and/or biophysical information. J. Am. Chem. Soc. 125 (2003) 1731-1737
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 9
    • 0037018912 scopus 로고    scopus 로고
    • Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD
    • Goulding C.W., Sawaya M.R., Parseghian A., Lim V., Eisenberg D., and Missiakas D. Thiol-disulfide exchange in an immunoglobulin-like fold: structure of the N-terminal domain of DsbD. Biochemistry 41 (2002) 6920-6927
    • (2002) Biochemistry , vol.41 , pp. 6920-6927
    • Goulding, C.W.1    Sawaya, M.R.2    Parseghian, A.3    Lim, V.4    Eisenberg, D.5    Missiakas, D.6
  • 10
    • 0037119945 scopus 로고    scopus 로고
    • The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDα complex
    • Haebel P.W., Goldstone D., Katzen F., Beckwith J., and Metcalf P. The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: crystal structure of the DsbC-DsbDα complex. EMBO J. 21 (2002) 4774-4784
    • (2002) EMBO J. , vol.21 , pp. 4774-4784
    • Haebel, P.W.1    Goldstone, D.2    Katzen, F.3    Beckwith, J.4    Metcalf, P.5
  • 12
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen F., and Beckwith J. Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103 (2000) 769-779
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 13
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., and Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14 (1996) 51-55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 14
    • 0037023730 scopus 로고    scopus 로고
    • Characterization of the methionine sulfoxide reductase activities of PilB, a probable virulence factor from Neisseria meningitidis
    • Olry A., Boschi-Muller S., Marraud M., Sanglier-Cianferani S., Van Dorsselear A., and Branlant G. Characterization of the methionine sulfoxide reductase activities of PilB, a probable virulence factor from Neisseria meningitidis. J. Biol. Chem. 277 (2002) 12016-12022
    • (2002) J. Biol. Chem. , vol.277 , pp. 12016-12022
    • Olry, A.1    Boschi-Muller, S.2    Marraud, M.3    Sanglier-Cianferani, S.4    Van Dorsselear, A.5    Branlant, G.6
  • 15
    • 4544258776 scopus 로고    scopus 로고
    • The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases
    • Porat A., Cho S.H., and Beckwith J. The unusual transmembrane electron transporter DsbD and its homologues: a bacterial family of disulfide reductases. Res. Microbiol. 155 (2004) 617-622
    • (2004) Res. Microbiol. , vol.155 , pp. 617-622
    • Porat, A.1    Cho, S.H.2    Beckwith, J.3
  • 17
    • 49749120953 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis
    • Quinternet M., Tsan P., Neiers F., Beaufils C., Boschi-Muller S., Averlant-Petit M.C., Branlant G., and Cung M.T. Solution structure and backbone dynamics of the reduced and oxidized forms of the N-terminal domain of PilB from Neisseria meningitidis. Biochemistry 47 (2008) 8577-8589
    • (2008) Biochemistry , vol.47 , pp. 8577-8589
    • Quinternet, M.1    Tsan, P.2    Neiers, F.3    Beaufils, C.4    Boschi-Muller, S.5    Averlant-Petit, M.C.6    Branlant, G.7    Cung, M.T.8
  • 23
    • 0033230589 scopus 로고    scopus 로고
    • Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli
    • Stewart E.J., Katzen F., and Beckwith J. Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli. EMBO J. 18 (1999) 5963-5971
    • (1999) EMBO J. , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 27
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • Williamson R.A., Carr M.D., Frenkiel T.A., Feeney J., and Freedman R.B. Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation. Biochemistry 36 (1997) 13882-13889
    • (1997) Biochemistry , vol.36 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 28
    • 16844365759 scopus 로고    scopus 로고
    • The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases
    • Wu J., Neiers F., Boschi-Muller S., and Branlant G. The N-terminal domain of PILB from Neisseria meningitidis is a disulfide reductase that can recycle methionine sulfoxide reductases. J. Biol. Chem. 280 (2005) 12344-12350
    • (2005) J. Biol. Chem. , vol.280 , pp. 12344-12350
    • Wu, J.1    Neiers, F.2    Boschi-Muller, S.3    Branlant, G.4
  • 29
    • 0030808350 scopus 로고    scopus 로고
    • Methods for measurement of intermolecular NOEs by multi-nuclear NMR spectroscopy: Application to an N-peptide:boxB RNA complex
    • Zwahlen C., Legault P., Vincent S., Greenblatt J., Konrat R., and Kay L.E. Methods for measurement of intermolecular NOEs by multi-nuclear NMR spectroscopy: Application to an N-peptide:boxB RNA complex. J. Am. Chem. Soc. 119 (1997) 6711-6721
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6711-6721
    • Zwahlen, C.1    Legault, P.2    Vincent, S.3    Greenblatt, J.4    Konrat, R.5    Kay, L.E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.