Premium
Crystal and solution structural studies of mouse phospholipid hydroperoxide glutathione peroxidase 4
Author(s) -
Janowski Robert,
Scanu Sandra,
Niessing Dierk,
Madl Tobias
Publication year - 2016
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x16013686
Subject(s) - phospholipid hydroperoxide glutathione peroxidase , gpx4 , selenocysteine , glutathione peroxidase , peroxidase , glutathione , biochemistry , phospholipid , chemistry , cysteine , gpx1 , microbiology and biotechnology , biology , enzyme , membrane
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.