Crystallization and preliminary X-ray diffraction analysis of Salmonella typhimurium uridine phosphorylase complexed with 5-fluorouracil.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 65(Pt 6): 601-3, 2009 Jun 01.
Article
in En
| MEDLINE
| ID: mdl-19478441
ABSTRACT
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Uridine Phosphorylase
/
X-Ray Diffraction
/
Fluorouracil
/
Antimetabolites, Antineoplastic
Language:
En
Journal:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Year:
2009
Document type:
Article
Affiliation country:
RUSSIA