Abstract
The determination of the first three-dimensional structure of a protein disulfide oxidoreductase from the archaeon Pyrococcus furiosus ( Pf PDO) has provided the first view of active site disulfides in an archaeal protein. It reveals a unique structural form compared to those of protein disulfide oxidoreductases in bacteria and eukarya. Protein disulfide oxidoreductases have been well studied in bacteria and eukarya. They are ubiquitous redox enzymes consisting of the families of thioredoxin, glutaredoxin, protein disulfide-isomerase (PDI), DsbA, and their homologs. These enzymes catalyze the formation, breakage, and rearrangement of protein disulfide bonds. These well-characterized protein disulfide oxidoreductases share a similarity in their three-dimensional structures: all of them use a common structural motif as the scaffold. The three-dimensional structure of intact PDI is not yet determined, but its amino acid sequence and tertiary domain structures have revealed it to be a multidomain protein.
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