Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4

Abstract

The mammalian glutathione peroxidase (GPx) family is a key component of the cellular antioxidative defence system. Within this family, GPx4 has unique features as it accepts a large class of hydroperoxy lipid substrates and has a plethora of biological functions, including sperm maturation, regulation of apoptosis and cerebral embryogenesis. In this paper, the structure of the cytoplasmic isoform of mouse phospholipid hydroperoxide glutathione peroxidase (O70325-2 GPx4) with selenocysteine 46 mutated to cysteine is reported solved at 1.8 Å resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.The crystal structure of mouse phospholipid hydroperoxide glutathione peroxidase 4 solved at 1.8 Å resolution and the first solution structural studies of a glutathione peroxidase protein are reported.