1g0t: Difference between revisions

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{{STRUCTURE_1g0t|  PDB=1g0t  |  SCENE=  }}  
{{STRUCTURE_1g0t|  PDB=1g0t  |  SCENE=  }}  


'''DSBC MUTANT C101S'''
===DSBC MUTANT C101S===




==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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==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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