2RGV

The crystal structure of PerR-Ox highlights 2-oxo-Histidine formation

2RGV の概要

• エントリーDOI: 10.2210/pdb2rgv/pdb
• 関連するPDBエントリー: 2FE3
• 分子名称: Peroxide operon regulator, ZINC ION (3 entities in total)
• 機能のキーワード: 2-oxo-histidine, perr-ox, cytoplasm, dna-binding, manganese, oxidation, repressor, transcription, transcription regulation, zinc, 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: 33105.81

構造登録者

Traore, D.A.K. (登録日: 2007-10-05, 公開日: 2008-10-14, 最終更新日: 2025-03-26)

主引用文献

Traore, D.A.,El Ghazouani, A.,Jacquamet, L.,Borel, F.,Ferrer, J.L.,Lascoux, D.,Ravanat, J.L.,Jaquinod, M.,Blondin, G.,Caux-Thang, C.,Duarte, V.,Latour, J.M.
Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein.
Nat.Chem.Biol., 5:53-59, 2009

PubMed Abstract: In Bacillus subtilis, PerR is a metal-dependent sensor of hydrogen peroxide. PerR is a dimeric zinc protein with a regulatory site that coordinates either Fe(2+) (PerR-Zn-Fe) or Mn(2+) (PerR-Zn-Mn). Though most of the peroxide sensors use cysteines to detect H(2)O(2), it has been shown that reaction of PerR-Zn-Fe with H(2)O(2) leads to the oxidation of one histidine residue. Oxidation of PerR leads to the incorporation of one oxygen atom into His37 or His91. This study presents the crystal structure of the oxidized PerR protein (PerR-Zn-ox), which clearly shows a 2-oxo-histidine residue in position 37. Formation of 2-oxo-histidine is demonstrated and quantified by HPLC-MS/MS. EPR experiments indicate that PerR-Zn-H37ox retains a significant affinity for the regulatory metal, whereas PerR-Zn-H91ox shows a considerably reduced affinity for the metal ion. In spite of these major differences in terms of metal binding affinity, oxidation of His37 and/or His91 in PerR prevents DNA binding.

PubMed: 19079268
DOI: 10.1038/nchembio.133

実験手法

X-RAY DIFFRACTION (2.05 Å)