Structural highlights
Function
PDP_BACSU Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate.[UniProtKB:P77836][1]
Publication Abstract from PubMed
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 A resolution, which is an improvement on the previously reported structure at 2.6 A resolution. The localization and position of imidazole in the nucleoside-binding site reflects the possible binding of ligands that possess an imidazole ring.
Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.,Balaev VV, Prokofev II, Gabdoulkhakov AG, Betzel C, Lashkov AA Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):193-197. doi:, 10.1107/S2053230X18002935. Epub 2018 Mar 22. PMID:29633966[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Saxild HH, Andersen LN, Hammer K. Dra-nupC-pdp operon of Bacillus subtilis: nucleotide sequence, induction by deoxyribonucleosides, and transcriptional regulation by the deoR-encoded DeoR repressor protein. J Bacteriol. 1996 Jan;178(2):424-34. PMID:8550462
- ↑ Balaev VV, Prokofev II, Gabdoulkhakov AG, Betzel C, Lashkov AA. Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate. Acta Crystallogr F Struct Biol Commun. 2018 Apr 1;74(Pt 4):193-197. doi:, 10.1107/S2053230X18002935. Epub 2018 Mar 22. PMID:29633966 doi:http://dx.doi.org/10.1107/S2053230X18002935
