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-α-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.

• Authors: Yasuhide Takashima, Eiichi Mizohata, Keiji Tokuoka, Sudaratana R Krungkrai, Yukiko Kusakari, Saki Konishi, Atsuko Satoh, Hiroyoshi Matsumura, Jerapan Krungkrai, Toshihiro Horii, Tsuyoshi Inoue
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 68 Issue Pt 2 Pg. 244-6 (Feb 01 2012) ISSN: 1744-3091 [Electronic] England
• PMID: 22298010 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Orotate Phosphoribosyltransferase

Topics

• Crystallization
• Crystallography, X-Ray
• Orotate Phosphoribosyltransferase (chemistry)
• Plasmodium falciparum (enzymology)