Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding - Archive ouverte HAL Access content directly
Journal Articles Molecular Microbiology Year : 2009

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

Abstract

P>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.

Dates and versions

hal-00730670 , version 1 (10-09-2012)

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Lilian Jacquamet, Daouda A. K. Traoré, Jean-Luc Ferrer, Olivier Proux, Denis Testemale, et al.. Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding. Molecular Microbiology, 2009, 73 (1), pp.20-31. ⟨10.1111/j.1365-2958.2009.06753.x⟩. ⟨hal-00730670⟩
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