title: 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.
authors.affiliation: Group Intracellular Transport and RNA Biology, Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
authors.forename: Robert
authors.initials: R
authors.lastname: Janowski
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
authors.forename: Sandra
authors.initials: S
authors.lastname: Scanu
authors.affiliation: Group Intracellular Transport and RNA Biology, Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
authors.forename: Dierk
authors.initials: D
authors.lastname: Niessing
authors.affiliation: Institute of Structural Biology, Helmholtz Zentrum München - German Research Center for Environmental Health, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany.
authors.forename: Tobias
authors.initials: T
authors.lastname: Madl
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D003545:Cysteine / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D005979:Glutathione Peroxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D051379:Mice; D008958:Models, Molecular; D009154:Mutation; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D010957:Plasmids / Q000737:chemistry / Q000378:metabolism; D000072756:Protein Conformation, alpha-Helical; D000072757:Protein Conformation, beta-Strand; D054730:Protein Interaction Domains and Motifs; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017279:Selenocysteine / Q000737:chemistry* / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D011994:Recombinant Proteins; D017279:Selenocysteine; D000080662:Phospholipid Hydroperoxide Glutathione Peroxidase; D005979:Glutathione Peroxidase; C000611332:glutathione peroxidase 4, mouse; D003545:Cysteine
keywords: NMR spectroscopy; phospholipid hydroperoxide glutathione peroxidase 4; reactive oxidative species; small-angle X-ray scattering