The prokaryotic enzyme DsbB may share key structural features with eukaryotic disulfide bond forming oxidoreductases.

ABSTRACT: Three different classes of thiol-oxidoreductases that facilitate the formation of protein disulfide bonds have been identified. They are the Ero1 and SOX/ALR family members in eukaryotic cells, and the DsbB family members in prokaryotic cells. These enzymes transfer oxidizing potential to the proteins PDI or DsbA, which are responsible for directly introducing disulfide bonds into substrate proteins during oxidative protein folding in eukaryotes and prokaryotes, respectively. A comparison of the recent X-ray crystal structure of Ero1 with the previously solved structure of the SOX/ALR family member Erv2 reveals that, despite a lack of primary sequence homology between Ero1 and Erv2, the core catalytic domains of these two proteins share a remarkable structural similarity. Our search of the

SUBMITTER: Sevier CS 

PROVIDER: S-EPMC2253379 | biostudies-literature | 2005 Jun

REPOSITORIES: biostudies-literature