Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin
Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin
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DOI：
10.1021/bi900440m
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发表时间：
2009-07-07
期刊：
影响因子：
2.9
通讯作者：
Jacquamet, Lilian
中科院分区：
文献类型：
--
作者：
Iwema, Thomas;Picciocchi, Antoine;Jacquamet, Lilian
谷胱甘肽（GRX）是一种氧化还原蛋白，它使用谷胱甘肽作为辅助因子，分为单硫醇和二硫醇两类。在每一类中，都有几种GRX被证明可以形成[Fe2S2]簇配位的同型二聚体。二硫醇GRX同二聚体被提出作为一种隔离形式，其铁硫簇作为氧化应激传感器。相比之下，单硫醇GRX同二聚体被认为是[Fe2S2]簇递送的支架。我们在这里展示了单硫醇GRX同二聚体（大肠杆菌GRX4）协调一个[Fe2S2]簇的结构，揭示了完整铁硫簇传递的结构基础。
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.