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首页> 外文期刊>Crystallography reports >Three-dimensional structure of E-Coli purine nucleoside phosphorylase at 0.99 resolution
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Three-dimensional structure of E-Coli purine nucleoside phosphorylase at 0.99 resolution

机译：E-Coli嘌呤核苷磷酸化酶在0.99分辨率下的三维结构

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摘要

Purine nucleoside phosphorylases (PNPs) catalyze the reversible phosphorolysis of nucleosides and are key enzymes involved in nucleotide metabolism. They are essential for normal cell function and can catalyze the transglycosylation. Crystals of E. coli PNP were grown in microgravity by the capillary counterdiffusion method through a gel layer. The three-dimensional structure of the enzyme was determined by the molecular-replacement method at 0.99 resolution. The structural features are considered, and the structure of E. coli PNP is compared with the structures of the free enzyme and its complexes with purine base derivatives established earlier. A comparison of the environment of the purine base in the complex of PNP with formycin A and of the pyrimidine base in the complex of uridine phosphorylase with thymidine revealed the main structural features of the base-binding sites. Coordinates of the atomic model determined with high accuracy were deposited in the Protein Data Bank (PDB_ID: 4RJ2).
机译：嘌呤核苷磷酸化酶（PNP）催化核苷的可逆磷酸分解，是参与核苷酸代谢的关键酶。它们对于正常细胞功能至关重要，并且可以催化转糖基化。通过毛细管反扩散法通过凝胶层在微重力下生长大肠杆菌PNP晶体。通过分子置换法以0.99的分辨率确定酶的三维结构。考虑了结构特征，并将大肠杆菌PNP的结构与游离酶及其与较早建立的嘌呤碱基衍生物的复合物的结构进行了比较。 PNP与甲霉素A的复合物中嘌呤碱基与尿苷磷酸化酶与胸苷的复合物中嘧啶碱基的环境比较表明，碱基结合位点的主要结构特征。以高精度确定的原子模型的坐标存储在蛋白质数据库（PDB_ID：4RJ2）中。

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