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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1
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Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1

机译：Cap-domain闭包允许不同的衬底识别由C2-type haloaciddehalogenase-like糖磷酸酶疟原虫恶性疟原虫HAD1

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摘要

Haloacid dehalogenases (HADs) are a large enzyme superfamily of more than 500 000 members with roles in numerous metabolic pathways. Plasmodium falciparum HAD1 (PfHAD1) is a sugar phosphatase that regulates the methylerythritol phosphate (MEP) pathway for isoprenoid synthesis in malaria parasites. However, the structural determinants for diverse substrate recognition by HADs are unknown. Here, crystal structures were determined of PfHAD1 in complex with three sugar phosphates selected from a panel of diverse substrates that it utilizes. Cap-open and cap-closed conformations are observed, with cap closure facilitating substrate binding and ordering. These structural changes define the role of cap movement within the major subcategory of C2 HAD enzymes. The structures of an HAD bound to multiple substrates identifies binding and specificity-determining residues that define the structural basis for substrate recognition and catalysis within the HAD superfamily. While the substrate-binding region of the cap domain is flexible in the open conformations, this region becomes ordered and makes direct interactions with the substrate in the closed conformations. These studies further inform the structural and biochemical basis for catalysis within a large superfamily of HAD enzymes with diverse functions.
机译：Haloacid dehalogenases(已经)是一个大的酶总科的500多000人角色在许多代谢途径。恶性疟原虫HAD1磷酸酶(PfHAD1)是一种糖调节methylerythritol磷酸盐疟疾(MEP)的类异戊二烯合成途径寄生虫。为不同的底物识别了未知的。PfHAD1在复杂的磷酸盐和三个糖从面板选择不同的基质它利用。构象观察,盖关闭促进基质绑定和排序。这些结构性变化定义的角色C2的主要子类内部流动酶。多个基板标识绑定和specificity-determining残留定义底物识别和结构依据催化中的总科。substrate-binding帽域的区域灵活开放的构象,这一地区变得有序,使直接交互衬底的封闭的构象。这些研究结构和进一步通知在大型生化催化的基础总科的酶与多样化功能。

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