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High‐resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae
Author(s) -
Maghool Shadi,
La Fontaine Sharon,
Maher Megan J.
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19003327
Subject(s) - saccharomyces cerevisiae , glutathione , redox , oxidoreductase , yeast , glutaredoxin , chemistry , thiol , crystallization , crystal structure , biochemistry , resolution (logic) , crystallography , biophysics , biology , enzyme , inorganic chemistry , organic chemistry , artificial intelligence , computer science
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 P 2 1 2 1 2 1 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 status of the protein.