Abstract
Bacteria adapt to elevated levels of Reactive Oxygen Species (ROS) by increasing the expression of defence and repair proteins, which is regulated by ROS responsive transcription factors. In Bacillus subtilis the zinc protein PerR, a peroxide sensor that binds DNA in the presence of a regulatory metal Mn2+ or Fe2+, mediates the adaptive response to H2O2. This study presents the first crystal structure of apo-PerR-Zn which shows that all four cysteine residues of the protein are involved in zinc co-ordination. The Zn(Cys)4 site locks the dimerization domain and stabilizes the dimer. Sequence alignment of PerR-like proteins supports that this structural site may constitute a distinctive feature of this class of peroxide stress regulators.
MeSH terms
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Bacillus subtilis / genetics
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Bacillus subtilis / metabolism*
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Binding Sites / genetics
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Crystallization / methods
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Crystallography, X-Ray / methods*
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Cysteine / chemistry
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Cysteine / genetics
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Cysteine / metabolism
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Dimerization
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Dithionitrobenzoic Acid / chemistry
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Gene Expression Regulation, Bacterial
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Models, Molecular
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Repressor Proteins / chemistry*
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Repressor Proteins / genetics
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Repressor Proteins / metabolism
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Transcription Factors / chemistry*
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Transcription Factors / genetics
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Transcription Factors / metabolism
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Zinc / chemistry*
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Zinc / metabolism
Substances
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Bacterial Proteins
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Repressor Proteins
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Transcription Factors
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peroxide repressor proteins
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Dithionitrobenzoic Acid
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Zinc
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Cysteine