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首页> 外文期刊>Acta crystallographica. Section D, Biological crystallography. >Structure-based identification of inositol polyphosphate 1-phosphatase from Entamoeba histolytica
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Structure-based identification of inositol polyphosphate 1-phosphatase from Entamoeba histolytica

机译：基于结构的识别肌醇多磷酸盐1-phosphatase从痢疾阿米巴

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摘要

Inositol polyphosphate 1-phosphatase from Entamoeba histolytica (EhIPPase) is an Mg2+-dependent and Li+-sensitive enzyme that catalyzes the hydrolysis of inositol 1,4-bisphosphate [Ins(1,4)P2] into myo-inositol 1-monophosphate and PO43-. In the present work, EhIPPase has been biochemically identified and its crystal structure has been determined in the presence of Mg2+ and PO43- at 2.5 angstrom resolution. This enzyme was previously classified as a 3 '(2 '), 5 '-bisphosphate nucleotidase in the NCBI, but its biochemical activity and structural analysis suggest that this enzyme behaves more like an inositol polyphosphate 1-phosphatase. The ability of EhIPPase to hydrolyze the smaller Ins(1,4) P2 better than the bulkier 3-phosphoadenosine 5'-phosphate (PAP) is explained on the basis of the orientations of amino-acid residues in the binding site. This structure is the first of its class to be determined from any protozoan parasite, and is the third to determined among all organisms, following its rat and bovine homologues. The three-dimensional fold of EhIPPase is similar to those of other members of the inositol monophosphatase superfamily, which also includes inositol monophosphatase, 3 '(2 '), 5 '-bisphosphate nucleotidase and fructose-1,6-bisphosphate 1-phosphatase. They all share conserved residues essential for metal binding and substrate hydrolysis, with the motif D-X-n-EE-X-n-DP(L) DG(S/T)-X-n-WD-X-n-GG. The structure is divided into two domains, namely alpha+beta and alpha/beta, and the substrate and metal ions bind between them. However, the ability of each enzyme class to act specifically on its cognate substrate is governed by the class-specific amino-acid residues at the active site.
机译：肌醇多磷酸盐1-phosphatase从痢疾阿米巴(EhIPPase)是一个Mg2 +端依赖和李+敏感的酶,这种酶肌醇的催化水解1, 4-bisphosphate (Ins(1、4)P2)肌醇1-monophosphate和PO43 -。EhIPPase已识别和生化反应其晶体结构决定的Mg2 +和PO43 - 2.5埃决议。作为一个3(2),5 '酮糖核苷酸酶NCBI,但其生化活动结构分析表明,这种酶表现得更像一个肌醇多磷酸盐1-phosphatase。水解小Ins(1、4)P2比笨重3-phosphoadenosine 5 '磷酸(PAP)解释的方向的基础上结合位点的氨基酸残基。结构的第一个类决定从任何原生动物寄生虫,第三,确定在所有生物中,老鼠和牛后同系物。EhIPPase类似的三维折叠肌醇的其他成员monophosphatase总科,其中还包括肌醇monophosphatase 3 (2), 5“酮糖核苷酸酶和的特性,6-bisphosphate 1-phosphatase。分享守恒的残留金属所必需的绑定和底物水解,主题D-X-n-EE-X-n-DP (L) DG -X-n-WD-X-n-GG (S / T)。结构分为两个领域,即α+β和α/β和衬底金属离子结合。每个酶类具体行动的能力在其同源基质是由职业专用氨基酸残基在活跃网站。

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