1fvj
From Proteopedia
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THE 2.06 ANGSTROM STRUCTURE OF THE H32Y MUTANT OF THE DISULFIDE BOND FORMATION PROTEIN (DSBA)
Overview
DsbA, a 21-kDa protein from Escherichia coli, is a potent oxidizing, disulfide catalyst required for disulfide bond formation in secreted, proteins. The active site of DsbA is similar to that of mammalian protein, disulfide isomerases, and includes a reversible disulfide bond formed from, cysteines separated by two residues (Cys30-Pro31-His32-Cys33). Unlike most, protein disulfides, the active-site disulfide of DsbA is highly reactive, and the oxidized form of DsbA is much less stable than the reduced form at, physiological pH. His32, one of the two residues between the active-site, cysteines, is critical to the oxidizing power of DsbA and to the relative, instability of the protein in the oxidized form. Mutation of this single, residue to tyrosine, serine, or leucine results in a ... [(full description)]
About this Structure
1FVJ is a [Single protein] structure of sequence from [Escherichia coli]. Structure known Active Sites: CAA and CAB. Full crystallographic information is available from [OCA].
Reference
Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability., Guddat LW, Bardwell JC, Glockshuber R, Huber-Wunderlich M, Zander T, Martin JL, Protein Sci. 1997 Sep;6(9):1893-900. PMID:9300489
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