Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum.

ABSTRACT: Orotate phosphoribosyltransferase (OPRT) catalyzes the Mg(2+)-dependent condensation of orotic acid (OA) with 5-?-D-phosphorylribose 1-diphosphate (PRPP) to yield diphosphate (PP(i)) and the nucleotide orotidine 5'-monophosphate. OPRT from Plasmodium falciparum produced in Escherichia coli was crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg(2+). The crystal exhibited tetragonal symmetry, belonging to space group P4(1) or P4(3), with unit-cell parameters a = b = 49.15, c = 226.94 Å. X-ray diffraction data were collected to 2.5 Å resolution at 100 K using a synchrotron-radiation source.

SUBMITTER: Takashima Y 

PROVIDER: S-EPMC3274414 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature