Structural highlights
Function
[GLRX4_ECOLI] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (Probable).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin.,Iwema T, Picciocchi A, Traore DA, Ferrer JL, Chauvat F, Jacquamet L Biochemistry. 2009 Jun 15. PMID:19505088[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Iwema T, Picciocchi A, Traore DA, Ferrer JL, Chauvat F, Jacquamet L. Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin. Biochemistry. 2009 Jun 15. PMID:19505088 doi:10.1021/bi900440m
