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首页> 外文期刊>Journal of chemical crystallography >Crystal structure of the C47S mutant of human peroxiredoxin 5
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Crystal structure of the C47S mutant of human peroxiredoxin 5

机译：人过氧化物酶5的C47S突变体的晶体结构

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摘要

In the crystal structure of the reduced form of the wild-type human peroxiredoxin 5, the presence of a benzoate ion in direct interaction with the peroxidatic cysteine (Cys 47) appeared as a rather intriguing feature since it is known that the benzoate ion can play the role of a specific hydroxyl radical scavenger. The crystal structure of the C47S mutant of the same enzyme has been crystallized in the tetragonal system, space group P4(1)2(1)2, with a = 65.65 Angstrom, c = 122.04 Angstrom. It confirms the presence of this benzoate ion in spite of the mutation into a serine of the Cys 47 residue to which the benzoate ion was directly linked in the wild-type structure. The benzoate ion seems to be stabilized by hydrophobic contacts on both sides of the aromatic ring. In this matter, the alpha5 helix, which is specific to peroxiredoxin 5 among mammalian peroxiredoxins, plays an important role. These hydrophobic contacts also allow to suggest why the benzoate ion disappears when the molecule is oxidized.
机译：在野生型人过氧化物酶5的还原形式的晶体结构中，与过氧化半胱氨酸（Cys 47）直接相互作用的苯甲酸酯离子的存在似乎是一个吸引人的特征，因为已知苯甲酸酯离子可以发挥作用特定的羟基自由基清除剂的作用。同一酶的C47S突变体的晶体结构已在四角形系统中结晶，空间群P4（1）2（1）2，a = 65.65埃，c = 122.04埃。尽管在野生型结构中苯甲酸根离子直接连接到Cys 47残基的丝氨酸突变，但它证实了该苯甲酸根离子的存在。苯甲酸根离子似乎可以通过芳香环两侧的疏水性接触来稳定。在此问题上，哺乳动物过氧化物氧还蛋白中的过氧化物酶毒素5特有的alpha5螺旋起着重要作用。这些疏水性接触还提示了为什么当分子被氧化时苯甲酸根离子消失。

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