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The human malaria parasite Plasmodiiun falciparum is responsible for the death of more than a million people each year. Plasmodium falciparum S-adenosyl-L-homocysteine hydrolase (PfSAHH) inhibitors are expected to provide a new type of chemotherapeutic agent against malaria. Here we report the crystal structure of PfSAHH complexed with the reaction product adenosine. Knowledge of the structure in combination with a structural comparison with human SAHH (HsSAHH) revealed that a single amino acid substitution between the PfSAHH and HsSAHH accounts for the differential interactions with nucleoside inhibitors. The structure should provide opportunities to design selective PfSAHH inhibitors.

Crystal Structure Analysis of a Hydrolase from Plasmodium Falciparum Oriented for the Development of Novel Antimalarials