6MWS

crystal structure of the reduced Grx1 from Saccharomyces cerevisiae

Summary for 6MWS

• Entry DOI: 10.2210/pdb6mws/pdb
• Descriptor: Glutaredoxin-1, SULFATE ION (3 entities in total)
• Functional Keywords: glutaredoxin 1, yeast saccharomyces cerevisiae, oxidoreductase
• Biological source: Saccharomyces cerevisiae S288c (Baker's yeast)
• Total number of polymer chains: 1
• Total formula weight: 12901.67

Authors

Maghool, S.,Maher, J.M. (deposition date: 2018-10-30, release date: 2019-05-15, Last modification date: 2020-01-01)

Primary citation

Maghool, S.,La Fontaine, S.,Maher, M.J.
High-resolution crystal structure of the reduced Grx1 from Saccharomyces cerevisiae.
Acta Crystallogr.,Sect.F, 75:392-396, 2019

PubMed Abstract: 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.

PubMed: 31045569
DOI: 10.1107/S2053230X19003327

Experimental method

X-RAY DIFFRACTION (1.22 Å)