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Title: Isolation, crystallization and preliminary crystallographic analysis of Salmonella typhimurium uridine phosphorylase crystallized with 2,2′-anhydrouridine

Abstract

S. typhimurium uridine phosphorylase has been isolated and crystallized in the presence of ligand. Uridine phosphorylase (UPh; EC 2.4.2.3) is a member of the pyrimidine nucleoside phosphorylase family of enzymes which catalyzes the phosphorolytic cleavage of the C—N glycoside bond of uridine, with the formation of ribose 1-phosphate and uracil. This enzyme has been shown to be important in the activation and catabolism of fluoropyrimidines. Modulation of its enzymatic activity may affect the therapeutic efficacy of chemotherapeutic agents. The structural investigation of the bacterial uridine phosphorylases, both unliganded and complexed with substrate/product analogues and inhibitors, may help in understanding the catalytic mechanism of the phosphorolytic cleavage of uridine. Salmonella typhimurium uridine phosphorylase has been crystallized with 2,2′-anhydrouridine. X-ray diffraction data were collected to 2.15 Å. Preliminary analysis of the diffraction data indicates that the crystal belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 88.52, b = 123.98, c = 133.52 Å. The solvent content is 45.51%, assuming the presence of one hexamer molecule per asymmetric unit.

Authors:
; ; ;  [1];  [2];  [3]; ;
  1. A. V. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskiy Prospect 59, 119333 Moscow (Russian Federation)
  2. Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Institutskaya Street 3, 142290 Pushchino, Moscow Region (Russian Federation)
  3. Institute fur Biochemie und Lebensmittelchemie, University of Hamburg, c/o DESY, Building 22, Notkestrasse 85, 22604 Hamburg (Germany)
Publication Date:
OSTI Identifier:
22360400
Resource Type:
Journal Article
Journal Name:
Acta Crystallographica. Section F
Additional Journal Information:
Journal Volume: 63; Journal Issue: Pt 10; Other Information: PMCID: PMC2339722; PMID: 17909287; PUBLISHER-ID: en5246; OAI: oai:pubmedcentral.nih.gov:2339722; Copyright (c) International Union of Crystallography 2007; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CLEAVAGE; CRYSTALLIZATION; CRYSTALS; LIGANDS; MODULATION; MOLECULES; PHOSPHATES; SOLVENTS; SPACE GROUPS; SUBSTRATES; X-RAY DIFFRACTION

Citation Formats

Timofeev, Vladimir I., Lashkov, Alexander A., Gabdoulkhakov, Azat G., Pavlyuk, Bogdan Ph., Kachalova, Galina S., Betzel, Christian, Morgunova, Ekaterina Yu., Zhukhlistova, Nadezhda E., and Mikhailov, Al’bert M., E-mail: amm@ns.crys.ras.ru. Isolation, crystallization and preliminary crystallographic analysis of Salmonella typhimurium uridine phosphorylase crystallized with 2,2′-anhydrouridine. United Kingdom: N. p., 2007. Web. doi:10.1107/S1744309107040560.
Timofeev, Vladimir I., Lashkov, Alexander A., Gabdoulkhakov, Azat G., Pavlyuk, Bogdan Ph., Kachalova, Galina S., Betzel, Christian, Morgunova, Ekaterina Yu., Zhukhlistova, Nadezhda E., & Mikhailov, Al’bert M., E-mail: amm@ns.crys.ras.ru. Isolation, crystallization and preliminary crystallographic analysis of Salmonella typhimurium uridine phosphorylase crystallized with 2,2′-anhydrouridine. United Kingdom. https://doi.org/10.1107/S1744309107040560
Timofeev, Vladimir I., Lashkov, Alexander A., Gabdoulkhakov, Azat G., Pavlyuk, Bogdan Ph., Kachalova, Galina S., Betzel, Christian, Morgunova, Ekaterina Yu., Zhukhlistova, Nadezhda E., and Mikhailov, Al’bert M., E-mail: amm@ns.crys.ras.ru. 2007. "Isolation, crystallization and preliminary crystallographic analysis of Salmonella typhimurium uridine phosphorylase crystallized with 2,2′-anhydrouridine". United Kingdom. https://doi.org/10.1107/S1744309107040560.
@article{osti_22360400,
title = {Isolation, crystallization and preliminary crystallographic analysis of Salmonella typhimurium uridine phosphorylase crystallized with 2,2′-anhydrouridine},
author = {Timofeev, Vladimir I. and Lashkov, Alexander A. and Gabdoulkhakov, Azat G. and Pavlyuk, Bogdan Ph. and Kachalova, Galina S. and Betzel, Christian and Morgunova, Ekaterina Yu. and Zhukhlistova, Nadezhda E. and Mikhailov, Al’bert M., E-mail: amm@ns.crys.ras.ru},
abstractNote = {S. typhimurium uridine phosphorylase has been isolated and crystallized in the presence of ligand. Uridine phosphorylase (UPh; EC 2.4.2.3) is a member of the pyrimidine nucleoside phosphorylase family of enzymes which catalyzes the phosphorolytic cleavage of the C—N glycoside bond of uridine, with the formation of ribose 1-phosphate and uracil. This enzyme has been shown to be important in the activation and catabolism of fluoropyrimidines. Modulation of its enzymatic activity may affect the therapeutic efficacy of chemotherapeutic agents. The structural investigation of the bacterial uridine phosphorylases, both unliganded and complexed with substrate/product analogues and inhibitors, may help in understanding the catalytic mechanism of the phosphorolytic cleavage of uridine. Salmonella typhimurium uridine phosphorylase has been crystallized with 2,2′-anhydrouridine. X-ray diffraction data were collected to 2.15 Å. Preliminary analysis of the diffraction data indicates that the crystal belongs to space group P2{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 88.52, b = 123.98, c = 133.52 Å. The solvent content is 45.51%, assuming the presence of one hexamer molecule per asymmetric unit.},
doi = {10.1107/S1744309107040560},
url = {https://www.osti.gov/biblio/22360400}, journal = {Acta Crystallographica. Section F},
issn = {1744-3091},
number = Pt 10,
volume = 63,
place = {United Kingdom},
year = {Mon Oct 01 00:00:00 EDT 2007},
month = {Mon Oct 01 00:00:00 EDT 2007}
}