Structure of the thioredoxin-like domain of yeast glutaredoxin 3.
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.
Gibson
Lydia M
LM
Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
Dingra
Nin N
NN
Outten
Caryn E
CE
Lebioda
Lukasz
L
D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D018360:Crystallography, X-Ray; D054477:Glutaredoxins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry*; D016415:Sequence Alignment; D013879:Thioredoxins / Q000737:chemistry*
D054477:Glutaredoxins; D029701:Saccharomyces cerevisiae Proteins; D013879:Thioredoxins