3F8N

Crystal structure of PerR-Zn-Mn

Summary for 3F8N

• Entry DOI: 10.2210/pdb3f8n/pdb
• Related: 2FE3 2RGV
• Descriptor: Peroxide operon regulator, MANGANESE (II) ION, ZINC ION, ... (4 entities in total)
• Functional Keywords: dna binding protein, helix-turn-helix, cytoplasm, dna-binding, manganese, oxidation, repressor, transcription, transcription regulation, zinc
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (By similarity): P71086
• Total number of polymer chains: 2
• Total formula weight: 33137.83

Authors

Traore, D.A.K.,Ferrer, J.-L.,Jacquamet, L.,Duarte, V.,Latour, J.-M. (deposition date: 2008-11-13, release date: 2009-06-16, Last modification date: 2023-11-01)

Primary citation

Jacquamet, L.,Traore, D.A.K.,Ferrer, J.-L.,Proux, O.,Testemale, D.,Hazemann, J.-L.,Nazarenko, E.,El Ghazouani, A.,Caux-Thang, C.,Duarte, V.,Latour, J.-M.
Structural characterization of the active form of PerR: insights into the metal-induced activation of PerR and Fur proteins for DNA binding
Mol.Microbiol., 73:20-31, 2009

PubMed Abstract: 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.

PubMed: 19508285
DOI: 10.1111/j.1365-2958.2009.06753.x

Experimental method

X-RAY DIFFRACTION (3.15 Å)