Balaev V V, Prokofev I I, Gabdoulkhakov A G, Betzel C, Lashkov A A
A. V. Shubnikov Institute of Crystallography, Leninsky Prospect 59, Moscow 119333, Russian Federation.
Laboratory for Structural Biology of Infection and Inflammation, University of Hamburg, Institute of Biochemistry and Molecular Biology, c/o DESY, Building 22a, Notkestrasse 83, Hamburg, Germany.
Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):193-197. doi: 10.1107/S2053230X18002935. Epub 2018 Mar 22.
Pyrimidine-nucleoside phosphorylase catalyzes the phosphorolytic cleavage of thymidine and uridine with equal activity. Investigation of this protein is essential for anticancer drug design. Here, the structure of this protein from Bacillus subtilis in complex with imidazole and sulfate is reported at 1.9 Å resolution, which is an improvement on the previously reported structure at 2.6 Å resolution. The localization and position of imidazole in the nucleoside-binding site reflects the possible binding of ligands that possess an imidazole ring.
嘧啶核苷磷酸化酶能以相同活性催化胸苷和尿苷的磷酸解裂解。对这种蛋白质的研究对于抗癌药物设计至关重要。在此，报道了来自枯草芽孢杆菌的这种蛋白质与咪唑和硫酸盐复合物的结构，分辨率为1.9 Å，相较于之前报道的2.6 Å分辨率的结构有所改进。咪唑在核苷结合位点的定位和位置反映了具有咪唑环的配体可能的结合情况。
