Crystallization and preliminary crystallographic analysis of orotidine 5'-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum.
作者信息
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
机构信息
Unit of Biochemistry, Department of Medical Science, Faculty of Science, Rangsit University, Patumthani 12000, Thailand.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt 6):542-5. doi: 10.1107/S1744309106015594. Epub 2006 May 31.
Abstract
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)).
摘要
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