We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli.
- Authors
McCarthy, Andrew A.; Haebel, Peter W.; Törrönen, Anneli; Rybin, Vladimir; Baker, Edward N.; Metcalf, Peter
- 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 × 23 kDa homodimer and has both protein disulfide isomerase and chaperone activity. We report the 1.9 Å 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.
- Subjects
BACTERIAL proteins; ESCHERICHIA coli; MICROSTRUCTURE; CHEMICAL bonds
- Publication
Nature Structural Biology, 2000, Vol 7, Issue 3, p196
- ISSN
1072-8368
- Publication type
Article