2b5e | pdb_00002b5e
Crystal Structure of Yeast Protein Disulfide Isomerase
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Overview
Protein disulfide isomerase plays a key role in catalyzing the folding of, secretory proteins. It features two catalytically inactive thioredoxin, domains inserted between two catalytically active thioredoxin domains and, an acidic C-terminal tail. The crystal structure of yeast PDI reveals that, the four thioredoxin domains are arranged in the shape of a twisted "U", with the active sites facing each other across the long sides of the "U.", The inside surface of the "U" is enriched in hydrophobic residues, thereby, facilitating interactions with misfolded proteins. The domain arrangement, active site location, and surface features strikingly resemble the, Escherichia coli DsbC and DsbG protein disulfide isomerases. Biochemical, studies demonstrate that all domains of PDI, including the C-terminal, tail, are required for full catalytic activity. The structure defines a, framework for rationalizing the differences between the two active sites, and their respective roles in catalyzing the formation and rearrangement, of disulfide bonds.
About this Structure
2B5E is a Single protein structure of sequence from Saccharomyces cerevisiae with BA and GOL as ligands. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.
Reference
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites., Tian G, Xiang S, Noiva R, Lennarz WJ, Schindelin H, Cell. 2006 Jan 13;124(1):61-73. PMID:16413482
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