Structural highlights
Function
[GLRX3_YEAST] Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Yeast glutaredoxin 3 (Grx3) is a cytosolic protein that regulates the activity of the iron-responsive transcriptional activator Aft1. This member of the monothiol glutaredoxin family contains a thioredoxin-like domain and a glutaredoxin-like domain, which both possess a monothiol active site. The crystal structure of the thioredoxin-like domain has been determined at 1.5 A resolution and represents the first published structure of this domain for the monothiol glutaredoxin family. The loop containing the signature motif WAxxC is partially disordered, indicating a greater degree of flexibility in this region compared with classical dithiol thioredoxins with a WCGPC active-site motif.
Structure of the thioredoxin-like domain of yeast glutaredoxin 3.,Gibson LM, Dingra NN, Outten CE, Lebioda L Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):927-32. Epub 2008, Aug 13. PMID:18703840[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gibson LM, Dingra NN, Outten CE, Lebioda L. Structure of the thioredoxin-like domain of yeast glutaredoxin 3. Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):927-32. Epub 2008, Aug 13. PMID:18703840 doi:10.1107/S0907444908021641
