1A8L

PROTEIN DISULFIDE OXIDOREDUCTASE FROM ARCHAEON PYROCOCCUS FURIOSUS

Summary for 1A8L

• Entry DOI: 10.2210/pdb1a8l/pdb
• Descriptor: PROTEIN DISULFIDE OXIDOREDUCTASE, ZINC ION (3 entities in total)
• Functional Keywords: oxidoreductase, pdi, thioredoxin fold
• Biological source: Pyrococcus furiosus
• Total number of polymer chains: 1
• Total formula weight: 25878.08

Authors

Ren, B.,Tibbelin, G.,Pascale, D.,Rossi, M.,Bartolucci, S.,Ladenstein, R. (deposition date: 1998-03-26, release date: 1999-03-30, Last modification date: 2024-10-16)

Primary citation

Ren, B.,Tibbelin, G.,de Pascale, D.,Rossi, M.,Bartolucci, S.,Ladenstein, R.
A protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus contains two thioredoxin fold units.
Nat.Struct.Biol., 5:602-611, 1998

PubMed 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.

PubMed: 9665175
DOI: 10.1038/862

Experimental method

X-RAY DIFFRACTION (1.9 Å)