Structure of the Bacillus subtilis OhrB hydroperoxide-resistance protein in a fully oxidized state.
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.
Cooper
David R
DR
Department of Molecular Physiology and Biological Physics, University of Virginia and the PSI2 Integrated Center for Structure-Function Innovation Charlottesville, Virginia 22908, USA.
Surendranath
Yogesh
Y
Devedjiev
Yancho
Y
Bielnicki
Jakub
J
Derewenda
Zygmunt S
ZS
D001412:Bacillus subtilis / Q000302:isolation & purification / Q000378:metabolism*; D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism*; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D003545:Cysteine; D016166:Free Radical Scavengers; D006861:Hydrogen Peroxide / Q000037:antagonists & inhibitors / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D050505:Mutant Proteins / Q000302:isolation & purification / Q000378:metabolism*; D010084:Oxidation-Reduction; D013237:Stereoisomerism
D001426:Bacterial Proteins; D016166:Free Radical Scavengers; D050505:Mutant Proteins; D006861:Hydrogen Peroxide; D003545:Cysteine