Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.

摘要: DsbC is one of five Escherichia coli proteins required for disulfide bond formation and thought to function as a isomerase during oxidative protein folding in the periplasm. 2 × 23 kDa homodimer has both chaperone activity. We report 1.9 A resolution crystal structure oxidized where Cys-X-X-Cys active sites form bonds. The molecule consists separate thioredoxin-like domains joined via hinged linker helices an N-terminal dimerization domain. hinges allow relative movement sites, broad uncharged cleft between them may be involved peptide binding foldase activities.