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

Author:

Takashima Yasuhide,Mizohata Eiichi,Tokuoka Keiji,Krungkrai Sudaratana R.,Kusakari Yukiko,Konishi Saki,Satoh Atsuko,Matsumura Hiroyoshi,Krungkrai Jerapan,Horii Toshihiro,Inoue Tsuyoshi

Abstract

Orotate phosphoribosyltransferase (OPRT) catalyzes the Mg2+-dependent condensation of orotic acid (OA) with 5-α-D-phosphorylribose 1-diphosphate (PRPP) to yield diphosphate (PPi) and the nucleotide orotidine 5′-monophosphate. OPRT fromPlasmodium falciparumproduced inEscherichia coliwas crystallized by the sitting-drop vapour-diffusion method in complex with OA and PRPP in the presence of Mg2+. The crystal exhibited tetragonal symmetry, belonging to space groupP41orP43, with unit-cell parametersa=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.

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

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