首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.
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A metal-binding site in the catalytic subunit of anaerobic ribonucleotide reductase.

机译:厌氧核糖核苷酸还原酶催化亚基中的金属结合位点。

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摘要

A Zn(Cys)(4) center has been found in the C-terminal region of the crystal structure of the anaerobic class III ribonucleotide reductase (RNR) from bacteriophage T4. The metal center is structurally related to the zinc ribbon motif and to rubredoxin and rubrerythrin. Mutant enzymes of the homologous RNR from Escherichia coli, in which the coordinating cysteines, conserved in almost all known class III RNR sequences, have been mutated into alanines, are shown to be inactive as the result of their inability to generate the catalytically essential glycyl radical. The possible roles of the metal center are discussed in relationship to the currently proposed reaction mechanism for generation of the glycyl radical in class III RNRs.
机译:在噬菌体T4的厌氧III类核糖核苷酸还原酶(RNR)的晶体结构的C端区域中发现了一个Zn(Cys)(4)中心。金属中心在结构上与锌带基序以及红氧还蛋白和红血球菌素有关。来自大肠杆菌的同源RNR的突变酶,由于几乎无法产生催化上必不可少的甘氨酰基团,在该酶中,几乎所有已知的III类RNR序列中保守的配位半胱氨酸均突变为丙氨酸。 。讨论了金属中心的可能作用,并与目前提出的在III类RNR中生成甘氨酰基的反应机理进行了讨论。

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