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.
Keywords:
NMR spectroscopy; phospholipid hydroperoxide glutathione peroxidase 4; reactive oxidative species; small-angle X-ray scattering.
MeSH terms
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Amino Acid Sequence
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Animals
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Cloning, Molecular
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Crystallography, X-Ray
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Cysteine / chemistry*
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Cysteine / metabolism
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Glutathione Peroxidase / chemistry*
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Glutathione Peroxidase / genetics
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Glutathione Peroxidase / metabolism
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Mice
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Models, Molecular
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Mutation
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Phospholipid Hydroperoxide Glutathione Peroxidase
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Plasmids / chemistry
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Plasmids / metabolism
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Protein Conformation, alpha-Helical
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Protein Conformation, beta-Strand
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Protein Interaction Domains and Motifs
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Selenocysteine / chemistry*
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Selenocysteine / metabolism
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Substrate Specificity
Substances
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Recombinant Proteins
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Selenocysteine
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Phospholipid Hydroperoxide Glutathione Peroxidase
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Glutathione Peroxidase
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glutathione peroxidase 4, mouse
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Cysteine