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 Å 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.
Published in Acta Crystallographica Section D: Biological Crystallography, Volume 64, Issue 9, 2008, pages 927-932.
Gibson, L.M., Dingra, N.N., Outten, C.E., & Lebioda, L. (2008). Structure of the thioredoxin-like domain of yeast glutaredoxin 3. Acta Crystallographica Section D: Biological Crystallography, 64(9), 927-932. DOI: 10.1107/S0907444908021641
© 2008 International Union of Crystallography.