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1G0T

DSBC MUTANT C101S

Summary for 1G0T
Entry DOI10.2210/pdb1g0t/pdb
Related1eej
DescriptorTHIOL:DISULFIDE INTERCHANGE PROTEIN DSBC, DI(HYDROXYETHYL)ETHER (3 entities in total)
Functional Keywordsthiol oxidoreductase, protein disulfide bond isomerase, thioredoxin fold, isomerase
Biological sourceEscherichia coli
Total number of polymer chains2
Total formula weight47050.02
Authors
Haebel, P.W.,Metcalf, P. (deposition date: 2000-10-09, release date: 2003-02-04, Last modification date: 2024-11-20)
Primary citationHaebel, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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