2ZZD

Recombinant thiocyanate hydrolase, air-oxidized form of holo-enzyme

2ZZD の概要

• エントリーDOI: 10.2210/pdb2zzd/pdb
• 関連するPDBエントリー: 2DD4 2DD5 2DXB 2DXC
• 分子名称: Thiocyanate hydrolase subunit alpha, Thiocyanate hydrolase subunit beta, Thiocyanate hydrolase subunit gamma, ... (8 entities in total)
• 機能のキーワード: scnase, hydrolase, cobalt, metalloprotein, sulfenic acid, sulfinic acid, nitrile hydratase, thiocyanate, carbonyl sulfide, claw setting, protein, enzyme, complex, model complex, non-corrin, post-translational modification, sulfenate, sulfinate, cysteine, oxidation, autocatalytic activation, air inactivation, metal-binding
• 由来する生物種: Thiobacillus thioparus; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 242389.22

構造登録者

Arakawa, T.,Kawano, Y.,Katayama, Y.,Yohda, M.,Odaka, M. (登録日: 2009-02-09, 公開日: 2009-10-13, 最終更新日: 2023-11-01)

主引用文献

Arakawa, T.,Kawano, Y.,Katayama, Y.,Nakayama, H.,Dohmae, N.,Yohda, M.,Odaka, M.
Structural Basis for Catalytic Activation of Thiocyanate Hydrolase Involving Metal-Ligated Cysteine Modification
J.Am.Chem.Soc., 131:14838-14843, 2009

PubMed Abstract: Thiocyanate hydrolase (SCNase) is a member of a family of nitrile hydratase proteins, each of which contains a unique noncorrin cobalt center with two post-translationally modified cysteine ligands, cysteine-sulfenic acid or -sulfenate (Cys-SO(H)), and cysteine-sulfininate (Cys-SO(2)(-)), respectively. We have found that a partially matured recombinant SCNase was activated during storage. The crystal structures of SCNase before and after storage demonstrated that Cys-SO(2)(-) modification of gammaCys131 proceeded to completion prior to storage, while Cys-SO(H) modification of gammaCys133 occurred during storage. SCNase activity was suppressed when gammaCys133 was further oxidized to Cys-SO(2)(-). The correlation between the catalytic activity and the extent of the gammaCys133 modification indicates that the cysteine sulfenic acid modification of gammaCys133 is of primary importance in determining the activity of SCNase.

PubMed: 19785438
DOI: 10.1021/ja903979s

実験手法

X-RAY DIFFRACTION (1.78 Å)