The disulfide bond isomerase DsbC is activated by an immunoglobulin-fold thiol oxidoreductase: Crystal structure of the DsbC-DsbDα complex

EMBO Journal

Volumn 21, Issue 18, 2002, Pages 4774-4784

  Haebel, Peter W ^a   Goldstone, David ^a   Katzen, Federico ^a   Beckwith, Jon ^a   Metcalf, Peter ^a  

^a UNIVERSITY OF AUCKLAND   (New Zealand)

Author keywords

Disulfide bond isomerase DsbC; Electron transporter DsbD; Oxidative protein folding; Reaction intermediate; Thiol oxidoreductase

Indexed keywords

IMMUNOGLOBULIN; OXIDOREDUCTASE; THIOL OXIDASE;

AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; COMPLEX FORMATION; CRYSTAL STRUCTURE; DISULFIDE BOND; ELECTRON TRANSPORT; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; GENE REARRANGEMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FOLDING;

AMINO ACID SEQUENCE; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DISULFIDES; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MULTIENZYME COMPLEXES; OXIDATION-REDUCTION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0037119945     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf489     Document Type: Article

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