Abstract
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.
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