Structural highlights
Function
[GLRX_BPT4] Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Nikkola M, Gleason FK, Eklund H. Reduction of mutant phage T4 glutaredoxins by Escherichia coli thioredoxin reductase. J Biol Chem. 1993 Feb 25;268(6):3845-9. PMID:8440680
