Open AccessCrystallization and preliminary X‐ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum
Author(s) -
Takashima Yasuhide,
Mizohata Eiichi,
Tokuoka Keiji,
Krungkrai Sudaratana R.,
Kusakari Yukiko,
Konishi Saki,
Satoh Atsuko,
Matsumura Hiroyoshi,
Krungkrai Jerapan,
Horii Toshihiro,
Inoue Tsuyoshi
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111043247
Subject(s) - plasmodium falciparum , chemistry , crystallization , crystallography , biology , malaria , organic chemistry , immunology
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 P 4 1 or P 4 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.