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首页> 外文期刊>Journal of Molecular Biology >The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle
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The complex structures of ATP sulfurylase with thiosulfate, ADP and chlorate reveal new insights in inhibitory effects and the catalytic cycle

机译：ATP硫酸化酶与硫代硫酸盐，ADP和氯酸盐的复杂结构揭示了抑制作用和催化循环的新见解

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摘要

TI-ic ubiquitous enzyme ATP sulfurylase (ATPS) catalyzes the primary step of intracellular sulfate activation, the formation of adenosine 5'-phosphosulfate (APS). It has been shown that the enzyme catalyzes the generation of APS from ATP and inorganic sulfate in vitro and in vivo, and that this reaction can be inhibited by a number of simple molecules. Here, we present the crystal structures of ATPS from the yeast Saccharomyces cerevisiae complexed with compounds that have inhibitory effects on the catalytic reaction of ATPS. Thiosulfate and ADP mimic the substrates sulfate and ATP in the active site, but are non-reactive and thus competitive inhibitors of the sulfurylase reaction. Chlorate is bound in a crevice between the active site and the intermediate domain III of the complex structure. It forms hydrogen bonds to residues of both domains and stabilizes a "closed" conformation, inhibiting the release of the reaction products APS and PPi. These new observations are evidence for the crucial role of the displacement mechanism for the catalysis by ATPS.
机译：TI-ic无处不在的酶ATP硫酸化酶（ATPS）催化细胞内硫酸盐活化的第一步，即5'-磷酸腺苷（APS）的形成。已经表明，该酶在体外和体内催化从ATP和无机硫酸盐生成APS，并且该反应可以被许多简单分子抑制。在这里，我们介绍了来自酵母的ATPS的晶体结构与对ATPS的催化反应具有抑制作用的化合物复合。硫代硫酸盐和ADP在活性位点模拟底物硫酸盐和ATP，但它们是非反应性的，因此是硫酰化酶反应的竞争性抑制剂。氯酸盐结合在活性位点和复杂结构的中间结构域III之间的缝隙中。它在两个结构域的残基上形成氢键并稳定“封闭”构象，从而抑制了反应产物APS和PPi的释放。这些新发现为ATPS催化置换机制的关键作用提供了证据。

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