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Volumn 136, Issue 2, 2001, Pages 162-166

Crystallization and initial crystallographic analysis of the disulfide bond isomerase DsbC in complex with the α domain of the electron transporter DsbD

Author keywords

Crystal dehydration; Disulfide bond isomerase; DsbC; DsbD; Reaction intermediate; Thiol oxidoreductase; Transmembrane electron transporter; X ray crystallography

Indexed keywords

CARRIER PROTEIN; ISOMERASE; MUTANT PROTEIN; SOLVENT;

EID: 0035782685     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2001.4430     Document Type: Article
Times cited : (20)

References (18)
  • 1
    • 0034714289 scopus 로고    scopus 로고
    • Disulfide bonds are generated by quinone reduction
    • Bader, M. W., Xie, T., Yu, C. A., and Bardwell, J. C. (2000) Disulfide bonds are generated by quinone reduction. J. Biol. Chem. 275, 26082-26088.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26082-26088
    • Bader, M.W.1    Xie, T.2    Yu, C.A.3    Bardwell, J.C.4
  • 2
    • 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. (2000) 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, 1099-1109.
    • (2000) Mol. Microbiol. , vol.35 , pp. 1099-1109
    • Chung, J.1    Chen, T.2    Missiakas, D.3
  • 3
    • 0028103275 scopus 로고
    • The CCP4 suites: Programs for protein crystallography
    • Collaborative Computing Project No.4 (CCP4) (1994) The CCP4 suites: Programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 4
    • 0034115404 scopus 로고    scopus 로고
    • Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli
    • Fabianek, R. A., Hennecke, H., and Thony-Meyer, L. (2000) Periplasmic protein thiol:disulfide oxidoreductases of Escherichia coli. FEMS Microbiol. Rev. 24, 303-316.
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 303-316
    • Fabianek, R.A.1    Hennecke, H.2    Thony-Meyer, L.3
  • 5
    • 0034194815 scopus 로고    scopus 로고
    • Pathways for protein disulphide bond formation
    • Frand, A. R., Cuozzo, J. W., and Kaiser, C. A. (2000) Pathways for protein disulphide bond formation. Trends Cell Biol. 10, 203-210.
    • (2000) Trends Cell Biol. , vol.10 , pp. 203-210
    • Frand, A.R.1    Cuozzo, J.W.2    Kaiser, C.A.3
  • 7
    • 0030787850 scopus 로고    scopus 로고
    • In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC
    • Joly, J. C., and Swartz, J. R. (1997) In vitro and in vivo redox states of the Escherichia coli periplasmic oxidoreductases DsbA and DsbC. Biochemistry 36, 10067-10072.
    • (1997) Biochemistry , vol.36 , pp. 10067-10072
    • Joly, J.C.1    Swartz, J.R.2
  • 8
    • 0034703766 scopus 로고    scopus 로고
    • Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade
    • Katzen, F., and Beckwith, J. (2000) Transmembrane electron transfer by the membrane protein DsbD occurs via a disulfide bond cascade. Cell 103, 769-779.
    • (2000) Cell , vol.103 , pp. 769-779
    • Katzen, F.1    Beckwith, J.2
  • 9
    • 0029165589 scopus 로고
    • Thioredoxin - A fold for all reasons
    • Martin, J. L. (1995) Thioredoxin - A fold for all reasons. Structure 3, 245-250.
    • (1995) Structure , vol.3 , pp. 245-250
    • Martin, J.L.1
  • 10
  • 11
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J. 13, 2013-2020.
    • (1994) EMBO J. , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 12
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. (1995) Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J. 14, 3415-3424.
    • (1995) EMBO J. , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collecting in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collecting in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0033212804 scopus 로고    scopus 로고
    • The Rossmann Fourier autoindexing algorithm in MOSFLM
    • Powell, H. R. (1999) The Rossmann Fourier autoindexing algorithm in MOSFLM. Acta Crystallogr. D Biol. Crystallogr. 55, 1690-1695.
    • (1999) Acta Crystallogr. D Biol. Crystallogr. , vol.55 , pp. 1690-1695
    • Powell, H.R.1
  • 15
    • 0030668672 scopus 로고    scopus 로고
    • Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin
    • Rietsch, A., Bessette, P., Georgiou, G., and Beckwith, J. (1997) Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin. J. Bacteriol. 179, 6602-6608.
    • (1997) J. Bacteriol. , vol.179 , pp. 6602-6608
    • Rietsch, A.1    Bessette, P.2    Georgiou, G.3    Beckwith, J.4
  • 16
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • Shevchik, V. E., Condemine, G., and Robert-Baudouy, J. (1994) Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity. EMBO J. 13, 2007-2012.
    • (1994) EMBO J. , vol.13 , pp. 2007-2012
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 17
    • 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. (1999) 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, 5963-5971.
    • (1999) EMBO J , vol.18 , pp. 5963-5971
    • Stewart, E.J.1    Katzen, F.2    Beckwith, J.3
  • 18
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S., and Creighton, T. E. (1995) Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli. Biochemistry 34, 5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.