| Literature DB >> 29633966 |
V V Balaev1, I I Prokofev1, A G Gabdoulkhakov1, C Betzel2, A A Lashkov1.
Abstract
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.Entities:
Keywords: Bacillus subtilis; X-ray analysis; imidazole; nucleoside phosphorylases; nucleosides; protein crystallography; pyrimidine-nucleoside phosphorylase
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Year: 2018 PMID: 29633966 PMCID: PMC5894104 DOI: 10.1107/S2053230X18002935
Source DB: PubMed Journal: Acta Crystallogr F Struct Biol Commun ISSN: 2053-230X Impact factor: 1.056