Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum.
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.
Division of Applied Chemistry, Graduate School of Engineering, Osaka University, Suita, Osaka, Japan.
Yasuhide
Y
Takashima
Eiichi
E
Mizohata
Keiji
K
Tokuoka
Sudaratana R
SR
Krungkrai
Yukiko
Y
Kusakari
Saki
S
Konishi
Atsuko
A
Satoh
Hiroyoshi
H
Matsumura
Jerapan
J
Krungkrai
Toshihiro
T
Horii
Tsuyoshi
T
Inoue
D003460:Crystallization; D018360:Crystallography, X-Ray; D009962:Orotate Phosphoribosyltransferase / Q000737:chemistry*; D010963:Plasmodium falciparum / Q000201:enzymology*
D009962:Orotate Phosphoribosyltransferase