Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase
Copyright policy )Structural Basis for the Decarboxylation of Orotidine 5'-Monophosphate (OMP) by Plasmodium Falciparum OMP Decarboxylase
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.
- Osaka University Japan
- Chulalongkorn University Thailand
- Department of Medical Sciences Thailand
- Rangsit University Thailand
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Lysine, Molecular Sequence Data, Orotidine-5'-Phosphate Decarboxylase, Plasmodium falciparum, Protozoan Proteins, Crystallography, X-Ray, Decarboxylation, Protein Structure, Tertiary, Apoenzymes, Animals, Amino Acid Sequence, Uridine Monophosphate, Protein Binding
Models, Molecular, Binding Sites, Sequence Homology, Amino Acid, Lysine, Molecular Sequence Data, Orotidine-5'-Phosphate Decarboxylase, Plasmodium falciparum, Protozoan Proteins, Crystallography, X-Ray, Decarboxylation, Protein Structure, Tertiary, Apoenzymes, Animals, Amino Acid Sequence, Uridine Monophosphate, Protein Binding
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