首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii
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Structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii

机译:厌氧性超嗜热古生热球菌过氧化物酶的结构

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The crystal structure of peroxiredoxin from the anaerobic hyperthermophilic archaeon Pyrococcus horikoshii (PhPrx) was determined at a resolution of 2.25 angstrom. The overall structure was a ring-type decamer consisting of five homodimers. Citrate, which was included in the crystallization conditions, was bound to the peroxidatic cysteine of the active site, with two O atoms of the carboxyl group mimicking those of the substrate hydrogen peroxide. PhPrx lacked the C-terminal tail that forms a 32-residue extension of the protein in the homologous peroxiredoxin from Aeropyrum pernix (ApPrx).
机译:确定厌氧超嗜热古生热球菌(Pyrococcus horikoshii)(PhPrx)中的过氧化物酶的晶体结构,分辨率为2.25埃。总体结构是由五个同二聚体组成的环型十聚体。包含在结晶条件中的柠檬酸盐与活性位点的过氧化半胱氨酸结合,羧基的两个O原子模拟底物过氧化氢的羧基。 PhPrx缺少C末端的尾巴,该尾巴形成了来自Aeropyrum pernix(ApPrx)的同源过氧化物酶中蛋白质的32个残基的延伸。

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