2B5E

Crystal Structure of Yeast Protein Disulfide Isomerase

Summary for 2B5E

• Entry DOI: 10.2210/pdb2b5e/pdb
• Related: 1A8Y 1EEJ 1MEK 1V57 2BJX 2TRX
• Descriptor: Protein disulfide-isomerase, BARIUM ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: protein disulfide isomerase, isomerase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Endoplasmic reticulum lumen (Potential): P17967
• Total number of polymer chains: 1
• Total formula weight: 56743.13

Authors

Schindelin, H.,Tian, G. (deposition date: 2005-09-28, release date: 2006-01-24, Last modification date: 2024-10-16)

Primary citation

Tian, G.,Xiang, S.,Noiva, R.,Lennarz, W.J.,Schindelin, H.
The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites.
Cell(Cambridge,Mass.), 124:61-73, 2006

PubMed Abstract: 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.

PubMed: 16413482
DOI: 10.1016/j.cell.2005.10.044

Experimental method

X-RAY DIFFRACTION (2.4 Å)