2FE3

The crystal structure of bacillus subtilis PerR-Zn reveals a novel Zn(Cys)4 Structural redox switch

Summary for 2FE3

• Entry DOI: 10.2210/pdb2fe3/pdb
• Descriptor: Peroxide operon regulator, ZINC ION (3 entities in total)
• Functional Keywords: oxidative stress regulator, dna binding protein
• Biological source: Bacillus subtilis
• Cellular location: Cytoplasm (By similarity): P71086
• Total number of polymer chains: 2
• Total formula weight: 33027.96

Authors

Traore, D.A.K. (deposition date: 2005-12-15, release date: 2006-12-19, Last modification date: 2024-02-14)

Primary citation

Traore, D.A.K.,El Ghazouani, A.,Ilango, S.,Dupuy, J.,Jacquamet, L.,Ferrer, J.-L.,Caux-Thang, C.,Duarte, V.,Latour, J.M.
Crystal structure of the apo-PerR-Zn protein from Bacillus subtilis.
Mol.Microbiol., 61:1211-1219, 2006

PubMed Abstract: 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 Mn2+ or Fe2+, mediates the adaptive response to H2O2. 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.

PubMed: 16925555
DOI: 10.1111/j.1365-2958.2006.05313.x

Experimental method

X-RAY DIFFRACTION (1.75 Å)