Unknown

Dataset Information

0

Crystallization and preliminary crystallographic analysis of orotidine 5'-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum.

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)).

SUBMITTER: Krungkrai SR 

PROVIDER: S-EPMC2243097 | biostudies-literature | 2006 Jun

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Crystallization and preliminary crystallographic analysis of orotidine 5'-monophosphate decarboxylase from the human malaria parasite Plasmodium falciparum.

Krungkrai Sudaratana R SR   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  

Acta crystallographica. Section F, Structural biology and crystallization communications 20060531 Pt 6

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 radiati  ...[more]

Similar Datasets

Unknown Re-refinement of Plasmodium falciparum orotidine 5'-monophosphate decarboxylase provides a clearer picture of an important malarial drug target.
| S-EPMC6168774 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of orotate phosphoribosyltransferase from the human malaria parasite Plasmodium falciparum.
| S-EPMC3274414 | biostudies-literature
Unknown Crystallization and preliminary X-ray crystallographic study of phosphoglucose isomerase from Plasmodium falciparum.
| S-EPMC2833051 | biostudies-literature
Unknown Bromophycolide A targets heme crystallization in the human malaria parasite Plasmodium falciparum.
| S-EPMC3381860 | biostudies-literature
Unknown Mechanism of OMP decarboxylation in orotidine 5'-monophosphate decarboxylase.
| S-EPMC3651880 | biostudies-literature
Unknown The crystal structure and mechanism of orotidine 5'-monophosphate decarboxylase.
| S-EPMC15744 | biostudies-literature
Unknown Protein-Ribofuranosyl Interactions Activate Orotidine 5'-Monophosphate Decarboxylase for Catalysis.
| S-EPMC8650221 | biostudies-literature
Unknown Substrate distortion contributes to the catalysis of orotidine 5'-monophosphate decarboxylase.
| S-EPMC3949427 | biostudies-literature
Unknown Novel interactions of fluorinated nucleotide derivatives targeting orotidine 5'-monophosphate decarboxylase.
| S-EPMC3083246 | biostudies-literature
Unknown Structural determinants for the inhibitory ligands of orotidine-5'-monophosphate decarboxylase.
| S-EPMC3124134 | biostudies-literature