2WCI

Structure of E. coli monothiol glutaredoxin GRX4 homodimer

Summary for 2WCI

• Entry DOI: 10.2210/pdb2wci/pdb
• Related: 1YKA
• Descriptor: GLUTAREDOXIN-4, FE2/S2 (INORGANIC) CLUSTER, GLUTATHIONE, ... (5 entities in total)
• Functional Keywords: redox-active center, iron-sulfur cluster scaffolder, fe2s2, homodimer, transport, glutathione, thioredoxin fold, electron transport
• Biological source: ESCHERICHIA COLI
• Cellular location: Cytoplasm: P0AC69
• Total number of polymer chains: 2
• Total formula weight: 30935.59

Authors

Iwema, T.,Picchiocci, A.,Traore, D.A.K.,Ferrer, J.-L.,Chauvat, F.,Jacquamet, L. (deposition date: 2009-03-12, release date: 2009-06-23, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)