1A8L: Protein Disulfide Oxidoreductase From Archaeon Pyrococcus Furiosus

Citation:
Abstract
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.
PDB ID: 1A8LDownload
MMDB ID: 55088
PDB Deposition Date: 1998/3/26
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.9  Å
Source Organism:
Similar Structures:
Biological Unit for 1A8L: dimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1A8L
Label Count Molecule
Proteins (2 molecules)
2
Protein Disulfide Oxidoreductase
Molecule annotation
Chemicals (2 molecules)
1
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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