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首页> 外文期刊>The Open Crystallography Journal >Effect of Free Water Molecules on the Structure of Mg-ATPDipyridylamineand Overview on Selected Metal-Adenosine TriphosphateStructures in Model Compounds and in Enzymes
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Effect of Free Water Molecules on the Structure of Mg-ATPDipyridylamineand Overview on Selected Metal-Adenosine TriphosphateStructures in Model Compounds and in Enzymes

机译：游离水分子对Mg-ATP二吡啶胺结构的影响以及模型化合物和酶中某些金属三磷酸腺苷结构的概述

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The X-ray diffraction (XRD) structures for new isoforms of [M(H2O)6]·[M(HATP)2]·2(HDPA)·xH2O, ATP =adenosine 5’-triphosphate, DPA = 2,2’-dipyridylamine, M = Mg(II), x = 6H2O, 1, M = Ca(II), x = 8H2O, 2 were determinedby using rotating anode on molybdenum target X-ray source and Kappa CCD with confocal focusing mirror. Theaccuracy of the presently refined structure for 1 is the highest reported so far based on agreement factors (R1 = 0.0579)and estimated standard deviations (esds) on geometrical parameters. The comparative analysis was extended to the structuresof other low molecular weight metal-triphosphate complexes, to the structures of metal-triphosphate-protein systemsas well as to computed models of metal-triphosphate complexes. The structures of 1 and 2 reported in this work show thaton changing the number of co-crystallized water molecules, the interaction of the metal to the phosphate chain (for 1)and the conformation of ribose (for 2) undergo subtle but significant changes. Interestingly, the vast majority ofMg-nucleoside triphosphate (NTP)-enzyme systems have similar pattern of coordination to the phosphate chain whencompared to 1 and 2. The three phosphate groups have variable M-O bond distances, depending on the systems. Thestructures for 1 and 2 have a high significance as general model compounds for experimental solid state and computationsfor these types of biological systems.
机译：[M（H2O）6]·[M（HATP）2]·2（HDPA）·xH2O的新同工型的X射线衍射（XRD）结构，ATP =腺苷5'-三磷酸酯，DPA = 2,2' -二吡啶基胺，M = Mg（II），x = 6H2O，1，M = Ca（II），x = 8H2O，2是通过在钼靶X射线源上旋转阳极和具有共聚焦镜的Kappa CCD来确定的。基于一致性因子（R1 = 0.0579）和几何参数的估计标准偏差（esds），目前针对1精炼的结构的准确性是迄今为止报道的最高值。比较分析扩展到其他低分子量金属三磷酸配合物的结构，金属三磷酸-蛋白质系统的结构以及金属三磷酸配合物的计算模型。这项工作中报道的1和2的结构表明，在改变共结晶水分子的数量时，金属与磷酸盐链的相互作用（对于1）和核糖的构象（对于2）发生了细微但显着的变化。有趣的是，与1和2相比，绝大多数Mg-核苷三磷酸（NTP）-酶系统具有与磷酸盐链相似的配位模式。这三个磷酸基团的M-O键距可变，具体取决于系统。 1和2的结构作为用于实验固态和此类生物系统计算的通用模型化合物具有很高的意义。

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