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

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• 作者：Robert Janowski ; Sandra Scanu ; Dierk Niessing and Tobias Madl
• 关键词：phospholipid hydroperoxide glutathione peroxidase 4 ; reactive oxidative species ; NMR spectroscopy ; small-angle X-ray scattering
• 刊名：Acta Crystallographica Section F
• 出版年：2016
• 出版时间：October 2016
• 年：2016
• 卷：72
• 期：10
• 页码：743-749
• 全文大小：919K
• ISSN：1744-3091

文摘

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.