1dsb
From Proteopedia
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CRYSTAL STRUCTURE OF THE DSBA PROTEIN REQUIRED FOR DISULPHIDE BOND FORMATION IN VIVO
Overview
Proteins that contain disulphide bonds are often slow to fold in vitro, because the oxidation and correct pairing of the cysteine residues is rate, limiting. The folding of such proteins is greatly accelerated in, Escherichia coli by DsbA, but the mechanism of this rate enhancement is, not well understood. Here we report the crystal structure of oxidized DsbA, and show that it resembles closely the ubiquitous redox protein, thioredoxin, despite very low sequence similarity. An important, difference, however, is the presence of another domain which forms a cap, over the thioredoxin-like active site of DsbA. The redox-active disulphide, bond, which is responsible for the oxidation of substrates, is thus at a, domain interface and is surrounded by grooves and exposed hydrophobic side, chains. These features suggest that DsbA might act by binding to partially, folded polypeptide chains before oxidation of cysteine residues.
About this Structure
1DSB is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Crystal structure of the DsbA protein required for disulphide bond formation in vivo., Martin JL, Bardwell JC, Kuriyan J, Nature. 1993 Sep 30;365(6445):464-8. PMID:8413591
Page seeded by OCA on Tue Nov 20 13:32:44 2007
