Crystal structure of the apo‐PerR‐Zn protein from Bacillus subtilis

Summary 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 regula...

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Bibliographic Details
Published in:Molecular microbiology 2006-09, Vol.61 (5), p.1211-1219
Main Authors: Traoré, Daouda A. K., El Ghazouani, Abdelnasser, Ilango, Sougandi, Dupuy, Jérôme, Jacquamet, Lilian, Ferrer, Jean‐Luc, Caux‐Thang, Christelle, Duarte, Victor, Latour, Jean‐Marc
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - genetics
Bacillus subtilis - metabolism
Bacteria
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Binding Sites - genetics
Biochemistry
Biological and medical sciences
Crystal structure
Crystallization - methods
Crystallography, X-Ray - methods
Cysteine - chemistry
Cysteine - genetics
Cysteine - metabolism
Dimerization
Dithionitrobenzoic Acid - chemistry
DNA repair
Fundamental and applied biological sciences. Psychology
Gene expression
Gene Expression Regulation, Bacterial
Microbiology
Models, Molecular
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Proteins
Repressor Proteins - chemistry
Repressor Proteins - genetics
Repressor Proteins - metabolism
Transcription Factors - chemistry
Transcription Factors - genetics
Transcription Factors - metabolism
Zinc - chemistry
Zinc - metabolism
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Summary:Summary 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.
ISSN:0950-382X
1365-2958
DOI:10.1111/j.1365-2958.2006.05313.x