Protein Family Models

This family is closely related to Pfam:PF02798. (from Pfam)

Date:

2024-08-14

Date:

2024-08-14

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. [1]. 11453697. 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 2001;310:907-918. [2]. 11741965. Characterization of Escherichia coli null mutants for glutaredoxin 2. Vlamis-Gardikas A, Potamitou A, Zarivach R, Hochman A, Holmgren A;. J Biol Chem 2002;277:10861-10868. (from Pfam)

Date:

2024-10-16

glutaredoxin 2 is an aytpical glutaredoxin that catalyzes the glutathione dependent protein disulfide reduction of certain substrates, primarily proteins involved in cellular redox regulation

Date:

2018-04-23

Gene:

grxB

Date:

2021-09-20

Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system [1]. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase [2], and may have more to do with resistance to redox stress [3].

Date:

2024-05-29