Structural highlights
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