3CTF

Crystal structure of oxidized GRX2

Summary for 3CTF

• Entry DOI: 10.2210/pdb3ctf/pdb
• Related: 3CTG
• Descriptor: Glutaredoxin-2 (2 entities in total)
• Functional Keywords: oxidized form, electron transport, mitochondrion, redox-active center, transit peptide, transport, oxidoreductase
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Cytoplasm: P17695
• Total number of polymer chains: 1
• Total formula weight: 14150.11

Authors

Yu, J.,Teng, Y.B.,Zhou, C.Z. (deposition date: 2008-04-14, release date: 2008-11-11, Last modification date: 2024-11-06)

Primary citation

Li, W.F.,Yu, J.,Ma, X.X.,Teng, Y.B.,Luo, M.,Tang, Y.J.,Zhou, C.Z.
Structural basis for the different activities of yeast Grx1 and Grx2.
Biochim.Biophys.Acta, 1804:1542-1547, 2010

PubMed Abstract: Yeast glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor. Although sharing the same dithiolic CPYC active site and a sequence identity of 64%, they have been proved to play different roles during oxidative stress and to possess different glutathione-disulfide reductase activities. To address the structural basis of these differences, we solved the crystal structures of Grx2 in oxidized and reduced forms, at 2.10 A and 1.50 A, respectively. With the Grx1 structures we previously reported, comparative structural analyses revealed that Grx1 and Grx2 share a similar GSH binding site, except for a single residue substitution from Asp89 in Grx1 to Ser123 in Grx2. Site-directed mutagenesis in combination with activity assays further proved this single residue variation is critical for the different activities of yeast Grx1 and Grx2.

PubMed: 20417731
DOI: 10.1016/j.bbapap.2010.04.010

Experimental method

X-RAY DIFFRACTION (2.1 Å)