Abstract
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.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacillus subtilis / isolation & purification
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Bacillus subtilis / metabolism*
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Catalytic Domain
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Crystallography, X-Ray
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Cysteine
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Free Radical Scavengers
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Hydrogen Peroxide / antagonists & inhibitors
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Hydrogen Peroxide / metabolism
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Models, Molecular
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Mutagenesis, Site-Directed
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Mutant Proteins / isolation & purification
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Mutant Proteins / metabolism*
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Oxidation-Reduction
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Stereoisomerism
Substances
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Bacterial Proteins
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Free Radical Scavengers
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Mutant Proteins
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Hydrogen Peroxide
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Cysteine