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1g0t

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{{STRUCTURE_1g0t| PDB=1g0t | SCENE= }}
{{STRUCTURE_1g0t| PDB=1g0t | SCENE= }}
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'''DSBC MUTANT C101S'''
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===DSBC MUTANT C101S===
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==Overview==
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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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{{ABSTRACT_PUBMED_10700276}}
==About this Structure==
==About this Structure==
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[[Category: Thiol oxidoreductase]]
[[Category: Thiol oxidoreductase]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
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Revision as of 01:13, 1 July 2008

Image:1g0t.png

Template:STRUCTURE 1g0t

DSBC MUTANT C101S

Template:ABSTRACT PUBMED 10700276

About this Structure

1G0T is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli., McCarthy AA, Haebel PW, Torronen A, Rybin V, Baker EN, Metcalf P, Nat Struct Biol. 2000 Mar;7(3):196-9. PMID:10700276

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