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Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state

✍ Scribed by Cooper, David R. ;Surendranath, Yogesh ;Devedjiev, Yancho ;Bielnicki, Jakub ;Derewenda, Zygmunt S.

Book ID: 104478365
Publisher: International Union of Crystallography
Year: 2007
Tongue: English
Weight: 707 KB
Volume: 63
Category: Article
ISSN: 0907-4449
DOI: 10.1107/s0907444907050226

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✦ Synopsis

The crystal structure of the fully oxidized form of the Bacillus subtilis organic hydroperoxide-resistance (OhrB) protein is reported at 2.1 A ˚resolution. The electron density reveals an intact catalytic disulfide bond (Cys55-Cys119) in each of the two molecules, which are intertwined into a canonical obligate dimer. However, the stereochemistry of the disulfides is unorthodox and strained, suggesting that they are sensitive to reducing agents. A deep solvent-accessible gorge reaching Cys55 may represent the access route for the reductant.

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