3D6I

Structure of the Thioredoxin-like Domain of Yeast Glutaredoxin 3

Summary for 3D6I

• Entry DOI: 10.2210/pdb3d6i/pdb
• Related: 1ERT
• Descriptor: Monothiol glutaredoxin-3, SULFATE ION (3 entities in total)
• Functional Keywords: thioredoxin-like, glutaredoxin, electron transport, redox-active center, transport, oxidoreductase
• Biological source: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• Total number of polymer chains: 2
• Total formula weight: 25338.23

Authors

Lebioda, L.,Gibson, L.M.,Dingra, N.N.,Outten, C.E. (deposition date: 2008-05-19, release date: 2008-09-02, Last modification date: 2024-10-30)

Primary citation

Gibson, L.M.,Dingra, N.N.,Outten, C.E.,Lebioda, L.
Structure of the thioredoxin-like domain of yeast glutaredoxin 3.
Acta Crystallogr.,Sect.D, 64:927-932, 2008

PubMed 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.

PubMed: 18703840
DOI: 10.1107/S0907444908021641

Experimental method

X-RAY DIFFRACTION (1.5 Å)