6mws | pdb_00006mws
crystal structure of the reduced Grx1 from Saccharomyces cerevisiae
Structural highlights
Function[GLRX1_YEAST] Multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.[1] [2] [3] Publication Abstract from PubMedGrx1, 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 A 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. High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.,Maghool S, La Fontaine S, Maher MJ Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):392-396. doi:, 10.1107/S2053230X19003327. Epub 2019 Apr 26. PMID:31045569[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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