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Biochemistry. 2009 Jul 7;48(26):6041-3. doi: 10.1021/bi900440m.

Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin.

Author information

1
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, 5075 CEA, CNRS, Universite Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France. thomas.iwema@ibs.fr

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.

PMID:
19505088
DOI:
10.1021/bi900440m
[Indexed for MEDLINE]

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