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Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.

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.

SUBMITTER: Balaev VV

PROVIDER: S-EPMC5894104 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature

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Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.

Balaev V V VV Prokofev I I II Gabdoulkhakov A G AG Betzel C C Lashkov A A AA

Acta crystallographica. Section F, Structural biology communications 20180322 Pt 4

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 b ...[more]

PMID: 29633966

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