1a8l

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[[Image:1a8l.gif|left|200px]]
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{{Seed}}
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{{STRUCTURE_1a8l| PDB=1a8l | SCENE= }}
{{STRUCTURE_1a8l| PDB=1a8l | SCENE= }}
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'''PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS'''
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===PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS===
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==Overview==
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Protein disulfide bond formation is a rate limiting step in protein folding and is catalyzed by enzymes belonging to the protein disulfide oxidoreductase superfamily, including protein disulfide isomerase (PDI) in eucarya and DsbA in bacteria. The first high resolution X-ray crystal structure of a protein disulfide oxidoreductase from the hyperthermophilic archaeon Pyrococcus furiosus reveals structural details that suggest a relation to eukaryotic PDI. The protein consists of two homologous structural units with low sequence identity. Each unit contains a thioredoxin fold with a distinct CXXC active site motif. The accessibilities of both active sites are rather different as are, very likely, their redox properties. The protein shows the ability to catalyze the oxidation of dithiols as well as the reduction of disulfide bridges.
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(as it appears on PubMed at http://www.pubmed.gov), where 9665175 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9665175}}
==About this Structure==
==About this Structure==
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[[Category: Pdi]]
[[Category: Pdi]]
[[Category: Thioredoxin fold]]
[[Category: Thioredoxin fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:22:44 2008''

Revision as of 13:22, 30 June 2008

Image:1a8l.png

Template:STRUCTURE 1a8l

PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS

Template:ABSTRACT PUBMED 9665175

About this Structure

1A8L is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

Reference

A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units., Ren B, Tibbelin G, de Pascale D, Rossi M, Bartolucci S, Ladenstein R, Nat Struct Biol. 1998 Jul;5(7):602-11. PMID:9665175

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