Member database | Pfam |
Pfam type | domain |
Short name | Glutaredoxin2_C |
Clan | GST_C |
Author | Kerrison ND;0000-0002-1471-953X |
Sequence Ontology | 0000417 |
Description
Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2, Swiss:P39811), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyse reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.
References
1. Characterization of Escherichia coli null mutants for glutaredoxin 2. Vlamis-Gardikas A, Potamitou A, Zarivach R, Hochman A, Holmgren A. J. Biol. Chem. 277, 10861-8, (2002). View articlePMID: 11741965
2. Solution structure of Escherichia coli glutaredoxin-2 shows similarity to mammalian glutathione-S-transferases. Xia B, Vlamis-Gardikas A, Holmgren A, Wright PE, Dyson HJ. J. Mol. Biol. 310, 907-18, (2001). View articlePMID: 11453697
Integrated to
Representative structure
7dkp: Crystal structure of E. coli Grx2 in complex with GSH at 1.45 A resolution