2WCI

Structure of E. coli monothiol glutaredoxin GRX4 homodimer

2WCI の概要

• エントリーDOI: 10.2210/pdb2wci/pdb
• 関連するPDBエントリー: 1YKA
• 分子名称: GLUTAREDOXIN-4, FE2/S2 (INORGANIC) CLUSTER, GLUTATHIONE, ... (5 entities in total)
• 機能のキーワード: redox-active center, iron-sulfur cluster scaffolder, fe2s2, homodimer, transport, glutathione, thioredoxin fold, electron transport
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cytoplasm: P0AC69
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30935.59

構造登録者

Iwema, T.,Picchiocci, A.,Traore, D.A.K.,Ferrer, J.-L.,Chauvat, F.,Jacquamet, L. (登録日: 2009-03-12, 公開日: 2009-06-23, 最終更新日: 2024-05-08)

主引用文献

Iwema, T.,Picciocchi, A.,Traore, D.A.K.,Ferrer, J.-L.,Chauvat, F.,Jacquamet, L.
Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin.
Biochemistry, 48:6041-, 2009

PubMed Abstract: Glutaredoxins (GRX) are redox proteins which use glutathione as a cofactor and are divided into two classes, monothiol and dithiol. In each class, several GRX have been shown to form [Fe2S2] cluster coordinating homodimers. The dithiol GRX homodimer is proposed to serve as a sequestration form and its iron-sulfur cluster as an oxidative stress sensor. In contrast, the monothiol GRX homodimer has been suggested to act as a scaffold for [Fe2S2] cluster delivery. We present here the structure of a monothiol GRX homodimer (Escherichia coli GRX4) coordinating a [Fe2S2] cluster that reveals the structural basis of intact iron-sulfur cluster delivery.

PubMed: 19505088
DOI: 10.1021/BI900440M

実験手法

X-RAY DIFFRACTION (1.9 Å)