2OE3

Crystal Structure of Mitochondrial Thioredoxin 3 from Saccharomyces cerevisiae (oxidized form)

2OE3 の概要

• エントリーDOI: 10.2210/pdb2oe3/pdb
• 関連するPDBエントリー: 2OE0 2OE1
• 分子名称: Thioredoxin-3 (2 entities in total)
• 機能のキーワード: electron transport, alpha/beta sandwich, oxidized, dimer
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Mitochondrion: P25372
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25737.87

構造登録者

Bao, R.,Zhang, Y.R.,Zhou, C.Z.,Chen, Y.X. (登録日: 2006-12-28, 公開日: 2008-01-08, 最終更新日: 2024-11-06)

主引用文献

Bao, R.,Zhang, Y.R.,Zhou, C.-Z.,Chen, Y.X.
Structural and mechanistic analyses of yeast mitochondrial thioredoxin Trx3 reveal putative function of its additional cysteine residues
Biochim.Biophys.Acta, 1794:716-721, 2009

PubMed Abstract: The yeast Saccharomyces cerevisiae Trx3 is a key member of the thioredoxin system to control the cellular redox homeostasis in mitochondria. We solved the crystal structures of yeast Trx3 in oxidized and reduced forms at 1.80 and 2.10 A, respectively. Besides the active site, the additional cysteine residue Cys69 also undergoes a significant redox-correlated conformational change. Comparative structural analyses in combination with activity assays revealed that residue Cys69 could be S-nitrosylated in vitro. S-nitrosylation of Cys69 will decrease the activity of Trx3 by 20%, which is comparable to the effect of the Cys69Ser mutation. Taken together, these findings provided us some new insights into the putative function of the additional cysteine residues of Trx3.

PubMed: 19166985
DOI: 10.1016/j.bbapap.2008.12.016

実験手法

X-RAY DIFFRACTION (1.8 Å)