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首页> 外文期刊>Crystallography reports >Structural and Functional Analysis of Pyrimidine Nucleoside Phosphorylases of the NP-I and NP-II Families in Complexes with 6-Methyluracil
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Structural and Functional Analysis of Pyrimidine Nucleoside Phosphorylases of the NP-I and NP-II Families in Complexes with 6-Methyluracil

机译：嘧啶嘧啶核苷酸酶的结构和功能性分析，6-甲基脲酸盐中的络合物中的NP-I和NP-II系列

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摘要

The structure of bacterial uridine phosphorylase (UPh) belonging to the NP-I family in complex with 6-methyluracil was determined for the first time at 1.17 A resolution. The structural features of bacterial UPh from the bacterium Vibrio cholerae (VchUPh) responsible for selectivity toward 6-methyluracil acting as a pseudosubstrate were revealed. The repulsion between the hydrophilic hydroxyl group of the active-site residue Thr93 of VchUPh and the hydrophobic methyl group of 6-methyluracil prevents the oxygen atom O4' of the ribose moiety and the phosphate oxygen atom O3P of ribose 1-phosphate from forming hydrogen bonds with OG1_Thr93, which are essential for the enzymatic reaction. This, apparently, makes VchUPh inactive in the enzymatic synthesis of 6-methyluridine from 6-methyluracil. Hence, Thr93 is the residue, the modification of which will allow VchUPh to catalyze the biotechnologically important synthesis of 6-methyluridine from 6-methyluracil. Taking into account high structural homology of the functionally significant regions of bacterial UPhs, this conclusion is also true for other bacterial UPhs. It was demonstrated that bacterial thymidine phosphorylases of the NP-II family cannot bind 6-methyluracil in a proper conformation required for the catalysis because of a close contact between the 6-methyl group and Phe210.
机译：在1.17分辨率下，第一次测定属于与6-甲基脲的NP-I系列属于NP-I系列的细菌尿苷磷酸化酶（UPH）的结构。揭示了负责朝向6-甲基脲酸的选择性的细菌UPH的结构特征。 6-甲基脲的疏水性甲基的活性位点残留物的亲水性羟基之间的排斥力可防止核糖部分的氧原子O4'和核糖1-磷酸盐的磷酸氧原子O3p形成氢键对于OG1_Thr93，这对于酶促反应至关重要。显然，这使得Vchuph在来自6-甲基脲酸的6-甲基瓜啶的酶合成中不活跃。因此，Thr93是残余物，其改性将允许vchuph催化来自6-甲基脲的6-甲基瓜啶的生物技术重要合成。考虑到细菌UPH的功能有效地区的高结构同源性，对于其他细菌UPH而言也是如此。证明，由于6-甲基和PHE210之间的紧密接触，NP-II家族的细菌胸苷磷酸酶不能在催化所需的适当构象中结合6-甲基浆菌。

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  • 来源
    《Crystallography reports》 |2018年第3期|共10页
  • 作者

    Prokofev I. I.; Lashkov A. A.; Gabdulkhakov A. G.; Balaev V. V.; Mironov A. S.; Betzel C.; Mikhailov A. M.;

  • 作者单位

    Russian Acad Sci Fed Sci Res Ctr Crystallog &

    Photon Shubnikov Inst Crystallog Moscow 119333 Russia;

    Russian Acad Sci Fed Sci Res Ctr Crystallog &

    Photon Shubnikov Inst Crystallog Moscow 119333 Russia;

    Russian Acad Sci Fed Sci Res Ctr Crystallog &

    Photon Shubnikov Inst Crystallog Moscow 119333 Russia;

    Russian Acad Sci Fed Sci Res Ctr Crystallog &

    Photon Shubnikov Inst Crystallog Moscow 119333 Russia;

    State Res Inst Genet &

    Select Ind Microorganisms Moscow 117545 Russia;

    Univ Hamburg D-20148 Hamburg Germany;

    Russian Acad Sci Fed Sci Res Ctr Crystallog &

    Photon Shubnikov Inst Crystallog Moscow 119333 Russia;

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  • 正文语种 eng
  • 中图分类 晶体学;
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