Open AccessCrystallization and preliminary crystallographic analysis of orotidine 5′‐monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum
Author(s) -
Krungkrai Sudaratana R.,
Tokuoka Keiji,
Kusakari Yukiko,
Inoue Tsuyoshi,
Adachi Hiroaki,
Matsumura Hiroyoshi,
Takano Kazufumi,
Murakami Satoshi,
Mori Yusuke,
Kai Yasushi,
Krungkrai Jerapan,
Horii Toshihiro
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106015594
Subject(s) - plasmodium falciparum , malaria , crystallization , parasite hosting , protozoa , chemistry , biology , biochemistry , genetics , immunology , organic chemistry , world wide web , computer science
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 ( Pf OMPDC) 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 Å resolution at 100 K using synchrotron radiation at the Swiss Light Source. The crystal exhibits trigonal symmetry (space group R 3), with hexagonal unit‐cell parameters a = b = 201.81, c = 44.03 Å. With a dimer in the asymmetric unit, the solvent content is 46% ( V M = 2.3 Å 3 Da −1 ).