2FE3

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

2FE3 の概要

• エントリーDOI: 10.2210/pdb2fe3/pdb
• 分子名称: Peroxide operon regulator, ZINC ION (3 entities in total)
• 機能のキーワード: oxidative stress regulator, dna binding protein
• 由来する生物種: Bacillus subtilis
• 細胞内の位置: Cytoplasm (By similarity): P71086
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33027.96

構造登録者

Traore, D.A.K. (登録日: 2005-12-15, 公開日: 2006-12-19, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.75 Å)