2ZA1

Crystal Structure of orotidine 5'-monophosphate decarboxylase complexed with orotidine 5'-monophosphate from P.falciparum

Summary for 2ZA1

• Entry DOI: 10.2210/pdb2za1/pdb
• Related: 2F84 2ZA2 2ZA3
• Descriptor: Orotidine 5'-phosphate decarboxylase, OROTIDINE-5'-MONOPHOSPHATE (3 entities in total)
• Functional Keywords: orotidine 5'-monophosphate decarboxylase, plasmodium falciparum, orotidine 5'-monophosphate, lyase, pyrimidine biosynthesis
• Biological source: Plasmodium falciparum (malaria parasite P. falciparum)
• Total number of polymer chains: 2
• Total formula weight: 76468.87

Authors

Tokuoka, K.,Inoue, T. (deposition date: 2007-09-26, release date: 2007-12-04, Last modification date: 2023-11-01)

Primary citation

Tokuoka, K.,Kusakari, Y.,Krungkrai, S.R.,Matsumura, H.,Kai, Y.,Krungkrai, J.,Horii, T.,Inoue, T.
Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase
J.BIOCHEM.(TOKYO), 143:69-78, 2008

PubMed Abstract: Orotidine 5'-monophoshate decarboxylase (OMPDC) catalyses the decarboxylation of orotidine 5'-monophosphate (OMP) to uridine 5'-monophosphate (UMP). Here, we report the X-ray analysis of apo, substrate or product-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.7, 2.65 and 2.65 A, respectively. The structural analysis provides the substrate recognition mechanism with dynamic structural changes, as well as the rearrangement of the hydrogen bond array at the active site. The structural basis of substrate or product binding to PfOMPDC will help to uncover the decarboxylation mechanism and facilitate structure-based optimization of antimalarial drugs.

PubMed: 17981823
DOI: 10.1093/jb/mvm193

Experimental method

X-RAY DIFFRACTION (2.65 Å)