Crystallization and preliminary X-ray diffraction analysis of Salmonella typhimurium uridine phosphorylase complexed with 5-fluorouracil.
Uridine phosphorylase (UPh; EC 2.4.2.3) catalyzes the phosphorolytic cleavage of the N-glycosidic bond of uridine to form ribose 1-phosphate and uracil. This enzyme also activates pyrimidine-containing drugs, including 5-fluorouracil (5-FU). In order to better understand the mechanism of the enzyme-drug interaction, the complex of Salmonella typhimurium UPh with 5-FU was cocrystallized using the hanging-drop vapour-diffusion method at 294 K. X-ray diffraction data were collected to 2.2 A resolution. Analysis of these data revealed that the crystal belonged to space group C2, with unit-cell parameters a = 158.26, b = 93.04, c = 149.87 A, alpha = gamma = 90, beta = 90.65 degrees . The solvent content was 45.85% assuming the presence of six hexameric molecules of the complex in the unit cell.
Lashkov
A A
AA
A. V. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninskiy Prospect 59, 119333 Moscow, Russia.
Gabdoulkhakov
A G
AG
Shtil
A A
AA
Mikhailov
A M
AM
D000964:Antimetabolites, Antineoplastic / Q000378:metabolism*; D001665:Binding Sites; D003460:Crystallization; D003625:Data Collection; D004926:Escherichia coli / Q000235:genetics; D005472:Fluorouracil / Q000378:metabolism*; D008958:Models, Molecular; D010957:Plasmids; D011485:Protein Binding; D012486:Salmonella typhimurium / Q000201:enzymology; D013223:Statistics as Topic; D013696:Temperature; D014169:Transformation, Bacterial; D014543:Uridine Phosphorylase / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D014867:Water / Q000378:metabolism; D014961:X-Ray Diffraction
D000964:Antimetabolites, Antineoplastic; D014867:Water; D014543:Uridine Phosphorylase; D005472:Fluorouracil