Maghool Shadi, La Fontaine Sharon, Maher Megan J
Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Melbourne, Victoria, Australia.
School of Life and Environmental Sciences, Deakin University, Melbourne, Victoria, Australia.
Acta Crystallogr F Struct Biol Commun. 2019 May 1;75(Pt 5):392-396. doi: 10.1107/S2053230X19003327. Epub 2019 Apr 26.
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 P222 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.
谷氧还蛋白1（Grx1）是一种胞质硫醇-二硫键氧化还原酶，它利用谷胱甘肽底物（还原型谷胱甘肽，GSH，和氧化型谷胱甘肽，GSSG）积极维持细胞的氧化还原稳态。本文报道了酿酒酵母（yGrx1）中还原型Grx1在空间群P222中的晶体结构，以及其结构解析和精修至1.22 Å分辨率的结果。为了研究酵母Grx1的结构-功能关系，将还原型yGrx1的晶体结构与氧化型和谷胱甘肽化形式的现有结构进行了比较。这些比较揭示了与Cys27-Cys30活性位点相邻的残基构象在蛋白质氧化还原状态改变时的结构差异。
