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

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.

SUBMITTER: Gibson LM

PROVIDER: S-EPMC2581515 | biostudies-literature | 2008 Sep

REPOSITORIES: biostudies-literature

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

Gibson Lydia M LM Dingra Nin N NN Outten Caryn E CE Lebioda Lukasz L

Acta crystallographica. Section D, Biological crystallography 20080813 Pt 9

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 conta ...[more]

PMID: 18703840

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