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Crystal structure of the apo‐PerR‐Zn protein from Bacillus subtilis
Author(s) -
Traoré Daouda A. K.,
El Ghazouani Abdelnasser,
Ilango Sougandi,
Dupuy Jérôme,
Jacquamet Lilian,
Ferrer JeanLuc,
CauxThang Christelle,
Duarte Victor,
Latour JeanMarc
Publication year - 2006
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2006.05313.x
Subject(s) - bacillus subtilis , biology , bacterial protein , microbiology and biotechnology , computational biology , biochemistry , bacteria , genetics , gene
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 Mn 2+ or Fe 2+ , mediates the adaptive response to H 2 O 2 . 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.