恶性疟原虫中乳清苷5'-单磷酸脱羧酶的结晶及初步晶体学分析
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.
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)).
乳清苷5'-单磷酸（OMP）脱羧酶（OMPDC；EC 4.1.1.23）催化尿苷5'-单磷酸（UMP）从头合成的最后一步，该酶的缺陷在恶性疟原虫中是致命的。活性重组恶性疟原虫OMPDC（PfOMPDC）通过接种法在悬滴中使用聚乙二醇3000作为沉淀剂进行结晶。在瑞士光源处使用同步辐射在100 K下收集了来自天然晶体的完整衍射数据，分辨率达到2.7 Å。该晶体呈现三方对称（空间群R3），六方晶胞参数a = b = 201.81，c = 44.03 Å。在不对称单元中有一个二聚体，溶剂含量为46%（V(M) = 2.3 Å3 Da(-1)）。
Zotero 插件