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Gene Review:

grxA - glutaredoxin 1

Escherichia coli CFT073

Kashima, Y. et al., Bacik, J.P. et al., Bushweller, J.H. et al., Bushweller, J.H. et al., Nikkola, M. et al., et al.

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Disease relevance of grxA

The determination of the nuclear magnetic resonance (NMR) solution structured of the mixed disulfide between the mutant Escherichia coli glutaredoxin Grx(C14S) and glutathione (GSH), Grx(C14S)-SG, is described, the binding site for GSH on Grx(C14S) is located, and the non-bonding interactions between -SG and the protein are characterized [1].
To study structure-function relationships of the vertebrate Grx-1 family, and reveal potential viral adaptations, we have determined crystal structures of the ectromelia virus glutaredoxin, EVM053, in the oxidized and reduced states [2].
The same relationship has been proposed for the glutaredoxin and R1 proteins expressed by all orthopoxviruses, including vaccinia, variola, and ectromelia virus [2].
The anti-Anabaena thioredoxin antibodies did react with another unusual thioredoxin-glutaredoxin produced by bacteriophage T4 [3].

High impact information on grxA

Even the glutaredoxin P66A, where the active-site cis-proline has been substituted, could be efficiently reduced by thioredoxin reductase [4].
Substitution of the aspartic acid at position 80 with a serine produced a glutaredoxin with superior activity [4].
Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry [5].
EVM053 also exhibits a novel cis-proline (Pro53) in a loop that has been shown to contribute to R1-binding in Escherichia coli Grx-1 [2].
The covalent structure of the mixed disulfide of glutaredoxin(C14S) with GSH prepared with 15N-labeling of the protein was confirmed with nuclear magnetic resonance (NMR) spectroscopy, establishing a basis for NMR structural studies of the glutathione binding site on glutaredoxin [6].

Chemical compound and disease context of grxA

In Escherichia coli glutaredoxin, the active site contains a redox-active disulfide/dithiol of the sequence Cys11-Pro12-Tyr13-Cys14 [6].

Other interactions of grxA

The redox protein from PH0178 had strong thioredoxin-like activity, but no glutaredoxin activity [7].

References

The nuclear magnetic resonance solution structure of the mixed disulfide between Escherichia coli glutaredoxin(C14S) and glutathione. Bushweller, J.H., Billeter, M., Holmgren, A., Wüthrich, K. J. Mol. Biol. (1994) [Pubmed]
Crystal Structures of a Poxviral Glutaredoxin in the Oxidized and Reduced States Show Redox-correlated Structural Changes. Bacik, J.P., Hazes, B. J. Mol. Biol. (2007) [Pubmed]
Activities of two dissimilar thioredoxins from the cyanobacterium Anabaena sp. strain PCC 7120. Gleason, F.K. J. Bacteriol. (1992) [Pubmed]
Reduction of mutant phage T4 glutaredoxins by Escherichia coli thioredoxin reductase. Nikkola, M., Gleason, F.K., Eklund, H. J. Biol. Chem. (1993) [Pubmed]
Glutaredoxin from rabbit bone marrow. Purification, characterization, and amino acid sequence determined by tandem mass spectrometry. Hopper, S., Johnson, R.S., Vath, J.E., Biemann, K. J. Biol. Chem. (1989) [Pubmed]
Structural and functional characterization of the mutant Escherichia coli glutaredoxin (C14----S) and its mixed disulfide with glutathione. Bushweller, J.H., Aslund, F., Wüthrich, K., Holmgren, A. Biochemistry (1992) [Pubmed]
A hyperthermostable novel protein-disulfide oxidoreductase is reduced by thioredoxin reductase from hyperthermophilic archaeon Pyrococcus horikoshii. Kashima, Y., Ishikawa, K. Arch. Biochem. Biophys. (2003) [Pubmed]

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