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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.

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APA Citation

Gibson, L., Dingra, N., Outten, C., & Lebioda, L. (2008). Structure of the Thioredoxin-like Domain of Yeast Glutaredoxin 3. Acta Crystallographica Section D: Biological Crystallography, 64(9), 927–932.


© Acta Crystallographica Section D: Biological Crystallography 2008, International Union of Crystallography.

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