1G0T

DSBC MUTANT C101S

Summary for 1G0T

• Entry DOI: 10.2210/pdb1g0t/pdb
• Related: 1eej
• Descriptor: THIOL:DISULFIDE INTERCHANGE PROTEIN DSBC, DI(HYDROXYETHYL)ETHER (3 entities in total)
• Functional Keywords: thiol oxidoreductase, protein disulfide bond isomerase, thioredoxin fold, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 47050.02

Authors

Haebel, P.W.,Metcalf, P. (deposition date: 2000-10-09, release date: 2003-02-04, Last modification date: 2024-11-20)

Primary citation

Haebel, P.W.,Goldstone, D.,Katzen, F.,Beckwith, J.,Metcalf, P.
Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli
Embo J., 21:4774-4784, 2002

PubMed 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.

PubMed: 10700276
DOI: 10.1093/emboj/cdf489

Experimental method

X-RAY DIFFRACTION (2.6 Å)