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

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.

Source: Acta Crystallographica Section F - September 21, 2016 Category: Biochemistry Authors: Janowski, R. Scanu, S. Niessing, D. Madl, T. Tags: phospholipid hydroperoxide glutathione peroxidase 4 reactive oxidative species NMR spectroscopy small-angle X-ray scattering research communications Source Type: research