PMID:10700276

Citation	McCarthy, AA, Haebel, PW, Törrönen, A, Rybin, V, Baker, EN and Metcalf, P (2000) Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7:196-9
Abstract	DsbC is one of five Escherichia coli proteins required for disulfide bond formation and is thought to function as a disulfide bond isomerase during oxidative protein folding in the periplasm. DsbC is a 2 x 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 A resolution crystal structure of oxidized DsbC where both Cys-X-X-Cys active sites form disulfide bonds. The molecule consists of separate thioredoxin-like domains joined via hinged linker helices to an N-terminal dimerization domain. The hinges allow relative movement of the active sites, and a broad uncharged cleft between them may be involved in peptide binding and DsbC foldase activities.
Links	PubMed Online version:10.1038/73295
Keywords	Amino Acid Sequence; Binding Sites; Catalytic Domain; Crystallization; Crystallography, X-Ray; Dimerization; Disulfides/metabolism; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Protein Disulfide-Isomerases/chemistry; Protein Disulfide-Isomerases/metabolism; Protein Folding; Protein Structure, Secondary; Solvents; Thioredoxins/metabolism
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