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Acta Crystallogr D Biol Crystallogr. 2008 Sep;64(Pt 9):927-32. doi: 10.1107/S0907444908021641. Epub 2008 Aug 13.

Structure of the thioredoxin-like domain of yeast glutaredoxin 3.

Author information

1
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.

Abstract

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.

PMID:
18703840
PMCID:
PMC2581515
DOI:
10.1107/S0907444908021641
[Indexed for MEDLINE]
Free PMC Article

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