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

Journal Article · · Acta Crystallographica. Section F
; ; ;  [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)

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.

OSTI ID:
22360400
Journal Information:
Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 10 Vol. 63; ISSN ACSFCL; ISSN 1744-3091
Country of Publication:
United Kingdom
Language:
English

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