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Background  The formation of a disulfide bond between two cysteine residues stabilizes protein structure. Although we now have a good understanding of the  Escherichia coli  disulfide formation system, the machineries at work in other bacteria, including pathogens, are poorly characterized. Thus, the objective of this work was to improve our understanding of the disulfide formation machinery of  Helicobacter pylori , a leading cause of ulcers and a risk factor for stomach cancer worldwide.    Methods and Results  The protein HP0231 from  H. pylori , a structural counterpart of  E. coli  DsbG, is the focus of this research. Its function was clarified by using a combination of biochemical, microbiological and genetic approaches. In particular, we determined the biochemical properties of HP0231 as well as its redox state in  H. pylori  cells.    Conclusion  Altogether our results show that HP0231 is an oxidoreductase that catalyzes disulfide bond formation in the periplasm. We propose to call it HpDsbA.

A Novel Insight into the Oxidoreductase Activity of Helicobacter pylori HP0231 Protein