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首页> 外文期刊>Biochemistry >Structural Characterization of the Stringent Response Related Exopolyphosphatase/ Guanosine Pentaphosphate Phosphohydrolase Protein Family
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Structural Characterization of the Stringent Response Related Exopolyphosphatase/ Guanosine Pentaphosphate Phosphohydrolase Protein Family

机译：严格反应相关的胞外磷酸酶/鸟苷五磷酸磷酸水解酶蛋白家族的结构表征

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摘要

Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation.The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined,providing the first insights to features of the common catalytic core of the PPX/GPPA family.The protein has a two-domain structure with an active site located in the interdomain cleft.Two crystal forms were investigated (type I and II) at resolutions of 1.53 and 2.15 A,respectively.This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins.A calcium ion is observed at the center of this region in type I crystals,substantiating that PPX/GPPA enzymes use metal ions for catalysis.Structural analysis suggests that nucleotides bind at a similar position to that seen in other members of the superfamily.
机译：外切磷酸酶/鸟嘌呤五磷酸鸟苷磷酸水解酶（PPX / GPPA）酶在饥饿引起的细菌严格反应中起着核心作用。已经确定了来自肌动蛋白样ATPase域超家族的推定的Aquifex aeolicus PPX / GPPA磷酸酶的高分辨率晶体结构，提供了对PPX / GPPA家族共同催化核心特征的初步见识。该蛋白质具有两个域结构，其活性位点位于域间裂隙中。研究了两种晶体形式（I型和II型）的分辨率为分别为1.53和2.15A。这揭示了一种结构柔性，该结构柔性以前被描述为其他肌动蛋白样超家族蛋白活性部位周围的“蝴蝶状”裂口。在该区域的中心观察到钙离子。 I型晶体，表明PPX / GPPA酶使用金属离子进行催化。结构分析表明，核苷酸的结合位置与其他超家族成员。

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