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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii.
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Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii.

机译：mannosyl-3-phosphoglycerate结构磷酸酶从海床horikoshii。

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摘要

Mannosyl-3-phosphoglycerate phosphatase (MPGP) catalyzes the dephosphorylation of alpha-mannosyl-3-phosphoglycerate (MPG) to produce alpha-mannosylglycerate (MG). In the hyperthermophile Pyrococcus horikoshii, MPGP plays a role in a series of enzyme reactions that are involved in the MG-biosynthesis pathway, which is important for maintaining life under conditions of high salt concentration. Crystal structures of P. horikoshii MPGP (PhoMPGP) in the holo form and in the apo form lacking the magnesium ion were determined by the multiple-wavelength anomalous diffraction method using SeMet-substituted PhoMPGP. PhoMPGP consists of two domains: a core domain that is conserved in the haloacid dehalogenase superfamily and a cap domain that is specific to the C2B cap subclass of the superfamily. Apo-form crystals contain two PhoMPGP molecules: one in the open conformation and the other in the closed conformation. In holo-form crystals both of the two molecules are in the closed conformation with phosphate and magnesium ions. PhoMPGP has a specific hairpin loop that is bent towards the active site in the closed conformation of both the apo and holo forms. PhoMPGP has a cavity between the two domains which is considered to be the substrate-binding site as a phosphate ion is located in the cavity, mimicking the binding manner of the phosphate group of MPG. The cavity is sequestered in the closed conformation such that a conformational change is indispensable for the release of products. A salt bridge from the general acid/base Asp10 to Arg170 is observed in the holo-form PhoMPGP which is not present in the open form. The importance of the conformational change in the activity of PhoMPGP is discussed.
机译：Mannosyl-3-phosphoglycerate磷酸酶(MPGP)催化的脱磷酸作用alpha-mannosyl-3-phosphoglycerate (MPG)生产alpha-mannosylglycerate(毫克)。在一系列的酶反应过程中发挥作用参与MG-biosynthesis通路,这是很重要的在维持生命吗高盐浓度的条件。结构的p . horikoshii MPGP (PhoMPGP)缺乏整体形式和apo形式镁离子是由多波长反常衍射方法使用SeMet-substituted PhoMPGP。两个领域:一个核心领域是守恒的在haloacid dehalogenase总科和特定于C2B帽帽域总科的子类。包含两个PhoMPGP分子:一个开放的构象和其他关闭构象。两个分子的构象与关闭磷和镁离子。特定的发夹弯向循环在封闭的构象活性部位人群和整体形式。被认为是两个域之间substrate-binding网站作为一个磷酸离子位于腔,模仿的绑定磷酸基的方式英里/加仑。隐藏在封闭的构象等构象变化是必不可少的发布的产品。一般酸/碱Asp10 Arg170中观察到的holo-form PhoMPGP中不存在开放的形式。PhoMPGP活性的变化进行了探讨。

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