Structural snapshots of OxyR reveal the peroxidatic mechanism of H₂O₂ sensing.

ABSTRACT: Hydrogen peroxide (H₂O₂) is a strong oxidant capable of oxidizing cysteinyl thiolates, yet only a few cysteine-containing proteins have exceptional reactivity toward H₂O₂ One such example is the prokaryotic transcription factor OxyR, which controls the antioxidant response in bacteria, and which specifically and rapidly reduces H₂O₂ In this study, we present crystallographic evidence for the H₂O₂-sensing mechanism and H₂O₂-dependent structural transition of Corynebacterium glutamicum OxyR by capturing the reduced and H₂O₂-bound structures of a serine mutant of the peroxidatic cysteine, and the full-length crystal structure of disulfide-bonded oxidized O

SUBMITTER: Pedre B 

PROVIDER: S-EPMC6294878 | biostudies-literature | 2018 Dec

REPOSITORIES: biostudies-literature