Crystallization and preliminary crystallographic analysis of orotidine 5'-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum.
Orotidine 5'-monophosphate (OMP) decarboxylase (OMPDC; EC 4.1.1.23) catalyzes the final step in the de novo synthesis of uridine 5'-monophosphate (UMP) and defects in the enzyme are lethal in the malaria parasite Plasmodium falciparum. Active recombinant P. falciparum OMPDC (PfOMPDC) was crystallized by the seeding method in a hanging drop using PEG 3000 as a precipitant. A complete set of diffraction data from a native crystal was collected to 2.7 A resolution at 100 K using synchrotron radiation at the Swiss Light Source. The crystal exhibits trigonal symmetry (space group R3), with hexagonal unit-cell parameters a = b = 201.81, c = 44.03 A. With a dimer in the asymmetric unit, the solvent content is 46% (V(M) = 2.3 A3 Da(-1)).
Krungkrai
Sudaratana R
SR
Unit of Biochemistry, Department of Medical Science, Faculty of Science, Rangsit University, Patumthani 12000, Thailand.
Tokuoka
Keiji
K
Kusakari
Yukiko
Y
Inoue
Tsuyoshi
T
Adachi
Hiroaki
H
Matsumura
Hiroyoshi
H
Takano
Kazufumi
K
Murakami
Satoshi
S
Mori
Yusuke
Y
Kai
Yasushi
Y
Krungkrai
Jerapan
J
Horii
Toshihiro
T
D000818:Animals; D003460:Crystallization; D009964:Orotidine-5'-Phosphate Decarboxylase / Q000737:chemistry*; D010963:Plasmodium falciparum / Q000201:enzymology*; D011994:Recombinant Proteins; D012997:Solvents; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D012997:Solvents; D009964:Orotidine-5'-Phosphate Decarboxylase