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Structural characterization of the active form of PerR: insights into the metal‐induced activation of PerR and Fur proteins for DNA binding
Author(s) -
Jacquamet L.,
Traoré D. A. K.,
Ferrer J.L.,
Proux O.,
Testemale D.,
Hazemann J.L.,
Nazarenko E.,
El Ghazouani A.,
CauxThang C.,
Duarte V.,
Latour J.M.
Publication year - 2009
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.1365-2958.2009.06753.x
Subject(s) - histidine , allosteric regulation , biology , bacillus subtilis , transcription factor , biochemistry , binding site , dna binding protein , dna , dna binding domain , protein structure , stereochemistry , amino acid , chemistry , genetics , gene , bacteria , receptor
Summary In Bacillus subtilis , the transcription factor PerR is an iron dependant sensor of H 2 O 2 . The sensing mechanism relies on a selective metal catalysed oxidation of two histidine residues of the regulatory site. Here we present the first crystal structure of the active PerR protein in complex with a Mn 2+ ion. In addition, X‐ray absorption spectroscopy experiments were performed to characterize the corresponding iron form of the protein. Both studies reveal a penta‐coordinate arrangement of the regulatory site that involves three histidines and two aspartates. One of the histidine ligand belongs to the N‐terminal domain. Binding of this residue to the regulatory metal allows the protein to adopt a caliper‐like conformation suited to DNA binding. Since this histidine is conserved in all PerR and a vast majority of Fur proteins, it is likely that the allosteric switch induced by the regulatory metal is general for this family of metalloregulators.