Structural characterization of the active form of PerR: Insights into the metal-induced activation of PerR and fur proteins for DNA binding

Lilian Jacquamet, Daouda A K Traore, Jean -Luc Ferrer, O Proux, Denis Testemale, Jean -Louis Hazemann, E Nazarenko, Abdelnasser El Ghazouani, Christelle Caux-Thang, Victor Duarte, Jean -Marc Latour

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In Bacillus subtilis, the transcription factor PerR is an iron dependant sensor of H2O2. 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 Mn2+ 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.
Original languageEnglish
Pages (from-to)20 - 31
Number of pages12
JournalMolecular Microbiology
Issue number1
Publication statusPublished - 2009
Externally publishedYes

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