High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae
Shadi Maghool, Sharon La Fontaine, Megan J Maher
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | INT UNION CRYSTALLOGRAPHY | Published : 2019
Grx1, a cytosolic thiol-disulfide oxidoreductase, actively maintains cellular redox homeostasis using glutathione substrates (reduced, GSH, and oxidized, GSSG). Here, the crystallization of reduced Grx1 from the yeast Saccharomyces cerevisiae (yGrx1) in space group P212121 and its structure solution and refinement to 1.22 Å resolution are reported. To study the structure-function relationship of yeast Grx1, the crystal structure of reduced yGrx1 was compared with the existing structures of the oxidized and glutathionylated forms. These comparisons revealed structural differences in the conformations of residues neighbouring the Cys27-Cys30 active site which accompany alterations in the redox..View full abstract
Awarded by ARC
This study was supported by ARC grant DP140102746 to MJM and an Australian Government Research Training Program Scholarship to SM.