cd03199

C-terminal, alpha helical domain of Glutaredoxin 2

CDD entry
Member databaseCDD
CDD typedomain
Short nameGST_C_GRX2
SetGST_C_family

Description

Glutathione S-transferase (GST) C-terminal domain family, Glutaredoxin 2 (GRX2) subfamily; composed of Escherichia coli GRX2 and similar proteins. Escherichia coli GRX2 is an atypical GRX with a molecular mass of about 24kD (most GRXs range from 9-12kD). It adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain, but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.
[2, 4, 5, 1, 3]

References

1.Expression of Escherichia coli glutaredoxin 2 is mainly regulated by ppGpp and sigmaS. Potamitou A, Neubauer P, Holmgren A, Vlamis-Gardikas A. J. Biol. Chem. 277, 17775-80, (2002). View articlePMID: 11889138

2.Glutaredoxins: glutathione-dependent redox enzymes with functions far beyond a simple thioredoxin backup system. Fernandes AP, Holmgren A. Antioxid. Redox Signal. 6, 63-74, (2004). View articlePMID: 14713336

3.The glutaredoxin -C-P-Y-C- motif: influence of peripheral residues. Foloppe N, Nilsson L. Structure 12, 289-300, (2004). View articlePMID: 14962389

4.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

5.Cloning, overexpression, and characterization of glutaredoxin 2, an atypical glutaredoxin from Escherichia coli. Vlamis-Gardikas A, Aslund F, Spyrou G, Bergman T, Holmgren A. J. Biol. Chem. 272, 11236-43, (1997). View articlePMID: 9111025

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