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Purification, crystallization and preliminary X-ray analysis of uridine phosphorylase from Salmonella typhimurium. 2004
Mariya V Dontsova, and
Yulia A Savochkina, and
Azat G Gabdoulkhakov, and
Sergey N Baidakov, and
Andrey V Lyashenko, and
Maria Zolotukhina, and
Liubov Errais Lopes, and
Mariya B Garber, and
Ekaterina Yu Morgunova, and
Stanislav V Nikonov, and
Alexandr S Mironov, and
Steven E Ealick, and
Al 'Bert M Mikhailov
Institute of Crystallography, Russian Academy of Sciences, Russia, and Institute of Protein Research, Russian Academy of Sciences, Russia.
The structural udp gene encoding uridine phosphorylase (UPh) was cloned from the Salmonella typhimurium chromosome and overexpressed in Escherichia coli cells. S. typhimurium UPh (StUPh) was purified to apparent homogeneity and crystallized. The primary structure of StUPh has high homology to the UPh from E. coli, but the enzymes differ substantially in substrate specificity and sensitivity to the polarity of the medium. Single crystals of StUPh were grown using hanging-drop vapor diffusion with PEG 8000 as the precipitant. X-ray diffraction data were collected to 2.9 A resolution. Preliminary analysis of the diffraction data indicated that the crystal belonged to space group P6(1(5)), with unit-cell parameters a = 92.3, c = 267.5 A. The solvent content is 37.7% assuming the presence of one StUPh hexamer per asymmetric unit.
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