2b5e

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{{STRUCTURE_2b5e| PDB=2b5e | SCENE= }}
{{STRUCTURE_2b5e| PDB=2b5e | SCENE= }}
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'''Crystal Structure of Yeast Protein Disulfide Isomerase'''
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===Crystal Structure of Yeast Protein Disulfide Isomerase===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 16413482 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16413482}}
==About this Structure==
==About this Structure==
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[[Category: Tian, G.]]
[[Category: Tian, G.]]
[[Category: Protein disulfide isomerase]]
[[Category: Protein disulfide isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:09:01 2008''

Revision as of 19:09, 27 July 2008

Image:2b5e.png

Template:STRUCTURE 2b5e

Crystal Structure of Yeast Protein Disulfide Isomerase

Template:ABSTRACT PUBMED 16413482

About this Structure

2B5E is a Single protein structure of sequence from Saccharomyces cerevisiae. 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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