Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 72, Issue -, Pages 743-749Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S2053230X16013686
Keywords
phospholipid hydroperoxide glutathione peroxidase 4; reactive oxidative species; NMR spectroscopy; small-angle X-ray scattering
Funding
- Deutsche Forschungsgemeinschaft [FOR 2333, SPP1935, SFB646]
- Bavarian Ministry of Sciences, Research and the Arts (Bavarian Molecular Biosystems Research Network)
- Deutsche Forschungsgemeinschaft [Emmy Noether program] [MA 5703/1-1]
- Deutsche Forschungsgemeinschaft [Excellence Initiative Center for Integrated Protein Science Munich (CIPSM)]
- Austrian Science Fund (FWF) [P28854, DK-MCD W1226]
- PhD programme 'Molecular Medicine' of the Medical University of Graz
- Austrian Science Fund (FWF) [P28854] Funding Source: Austrian Science Fund (FWF)
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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 angstrom resolution using X-ray crystallography. Furthermore, solution data of an isotope-labelled GPx protein are presented.
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