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Crystal structure of pyrimidine-nucleoside phosphorylase from Bacillus subtilis in complex with imidazole and sulfate.
Balaev, V V; Prokofev, I I; Gabdoulkhakov, A G; Betzel, C; Lashkov, A A.
Afiliação
  • Balaev VV; A. V. Shubnikov Institute of Crystallography, Leninsky Prospect 59, Moscow 119333, Russian Federation.
  • Prokofev II; A. V. Shubnikov Institute of Crystallography, Leninsky Prospect 59, Moscow 119333, Russian Federation.
  • Gabdoulkhakov AG; A. V. Shubnikov Institute of Crystallography, Leninsky Prospect 59, Moscow 119333, Russian Federation.
  • Betzel C; 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.
  • Lashkov AA; A. V. Shubnikov Institute of Crystallography, Leninsky Prospect 59, Moscow 119333, Russian Federation.
Acta Crystallogr F Struct Biol Commun ; 74(Pt 4): 193-197, 2018 04 01.
Article em En | MEDLINE | ID: mdl-29633966
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 Šresolution, which is an improvement on the previously reported structure at 2.6 Šresolution. The localization and position of imidazole in the nucleoside-binding site reflects the possible binding of ligands that possess an imidazole ring.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Sulfatos / Bacillus subtilis / Pirimidina Fosforilases / Imidazóis Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2018 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Sulfatos / Bacillus subtilis / Pirimidina Fosforilases / Imidazóis Idioma: En Revista: Acta Crystallogr F Struct Biol Commun Ano de publicação: 2018 Tipo de documento: Article