Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli |
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Authors: | McCarthy A A Haebel P W Törrönen A Rybin V Baker E N Metcalf P |
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Institution: | School of Biological Sciences, Auckland University, Private Bag 92019 Auckland New Zealand. |
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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. |
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