3CTF

Crystal structure of oxidized GRX2

3CTF の概要

• エントリーDOI: 10.2210/pdb3ctf/pdb
• 関連するPDBエントリー: 3CTG
• 分子名称: Glutaredoxin-2 (2 entities in total)
• 機能のキーワード: oxidized form, electron transport, mitochondrion, redox-active center, transit peptide, transport, oxidoreductase
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Cytoplasm: P17695
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14150.11

構造登録者

Yu, J.,Teng, Y.B.,Zhou, C.Z. (登録日: 2008-04-14, 公開日: 2008-11-11, 最終更新日: 2024-11-06)

主引用文献

Li, W.F.,Yu, J.,Ma, X.X.,Teng, Y.B.,Luo, M.,Tang, Y.J.,Zhou, C.Z.
Structural basis for the different activities of yeast Grx1 and Grx2.
Biochim.Biophys.Acta, 1804:1542-1547, 2010

PubMed Abstract: Yeast glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor. Although sharing the same dithiolic CPYC active site and a sequence identity of 64%, they have been proved to play different roles during oxidative stress and to possess different glutathione-disulfide reductase activities. To address the structural basis of these differences, we solved the crystal structures of Grx2 in oxidized and reduced forms, at 2.10 A and 1.50 A, respectively. With the Grx1 structures we previously reported, comparative structural analyses revealed that Grx1 and Grx2 share a similar GSH binding site, except for a single residue substitution from Asp89 in Grx1 to Ser123 in Grx2. Site-directed mutagenesis in combination with activity assays further proved this single residue variation is critical for the different activities of yeast Grx1 and Grx2.

PubMed: 20417731
DOI: 10.1016/j.bbapap.2010.04.010

実験手法

X-RAY DIFFRACTION (2.1 Å)