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There are an estimated 300-500 million cases of malaria and up to 3 million people die from this disease annually. Plasmodium falciparum is the causative agent of the most lethal and sever form of human malaria. Chemotherapy of malaria is available, but is complicated by both adverse effects and widespread resistance to most of the currently available anti-malaria drugs. The malaria parasite depends on de novo synthesis of pyrimidine nucleotides, whereas the human host has the ability to synthesize them by both de novo and salvage pathways. The de novo pathway contains six reaction steps. In the final two steps, uridine 5’-monophosphate (UMP) requires the addition of a ribose phosphate moiety from 5-phosphoribosyl-1-pyrophosphate to orotate by orotate phosphoribosyltransferase (OPRT) to form orotidine 5’-monophosphate (OMP) and pyrophosphate (PPi), and the subsequently decarboxylation of OMP to form UMP, by OMP decarboxylase (OMPDC). Here, we report the X-ray analysis of OMP or UMP-complex forms of OMPDC from Plasmodium falciparum (PfOMPDC) at 2.65 Å resolution. The structural analysis provides the substrate recognition mechanism with dynamic structural changes. And anti-malaria drugs design by using the structure of OMPDC is in progress.

Structural study of enzyme inhibitor complexes of eukaryotic glutamine synthetase fromZea mays