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首页> 外文期刊>Crystallography reports >Structure of a Complex of Uridine Phosphorylase from Yersinia pseudotuberculosis with the Modified Bacteriostatic Antibacterial Drug Determined by X-ray Crystallography and Computer Analysis
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Structure of a Complex of Uridine Phosphorylase from Yersinia pseudotuberculosis with the Modified Bacteriostatic Antibacterial Drug Determined by X-ray Crystallography and Computer Analysis

机译：X射线晶体学和计算机分析确定的假结核耶尔森氏菌尿苷磷酸化酶与修饰的抑菌抗菌药物配合物的结构

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摘要

Pseudotuberculosis and bubonic plague are acute infectious diseases caused by the bacteria Yersinia pseudotuberculosis and Yersinia pestis. These diseases are treated, in particular, with trimethoprim and its modified analogues. However, uridine phosphorylases (pyrimidine nucleoside phosphorylases) that are present in bacterial cells neutralize the action of trimethoprim and its modified analogues on the cells. In order to reveal the character of the interaction of the drug with bacterial uridine phosphorylase, the atomic structure of the unligated molecule of uridine-specific pyrimidine nucleoside phosphorylase from Yersinia pseudotuberculosis (YptUPh) was determined by X-ray diffraction at 1.7 resolution with high reliability (R-work = 16.2, R-free = 19.4%; r.m.s.d. of bond lengths and bond angles are 0.006 and 1.005 angstrom, respectively; DPI = 0.107 ). The atoms of the amino acid residues of the functionally important secondary-structure elements-the loop L9 and the helix H8-of the enzyme YptUPh were located. The three-dimensional structure of the complex of YptUPh with modified trimethoprim-referred to as 53I-was determined by the computer simulation. It was shown that 53I is a pseudosubstrate of uridine phosphorylases, and its pyrimidine-2,4-diamine group is located in the phosphate-binding site of the enzyme YptUPh.
机译：伪结核和鼠疫是由细菌耶尔森氏假结核和鼠疫耶尔森氏菌引起的急性传染病。这些疾病尤其用甲氧苄啶及其修饰的类似物治疗。但是，细菌细胞中存在的尿苷磷酸化酶（嘧啶核苷磷酸化酶）会中和甲氧苄啶及其修饰类似物对细胞的作用。为了揭示药物与细菌尿苷磷酸化酶相互作用的特性，通过X射线衍射以1.7的分辨率高可靠性地确定了来自耶尔森氏假结核耶尔森氏菌的尿苷特异性嘧啶核苷磷酸化酶的未连接分子的原子结构。 （R-功＝ 16.2，无R ＝ 19.4％;键长和键角的均方根分别为0.006和1.005埃; DPI ＝ 0.107）。确定了酶YptUPh的功能重要的二级结构元件-环L9和螺旋H8-的氨基酸残基的原子。通过计算机模拟确定了YptUPh与修饰的甲氧苄氨嘧啶的复合物的三维结构（称为53I）。结果表明53I是尿苷磷酸化酶的假底物，其嘧啶-2，4-二胺基位于酶YptUPh的磷酸结合位点。

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