Hsp90 is an important cellular chaperone and attractive target for therapeutics 
against both cancer and infectious organisms. The Hsp90 protein from the 
parasite Plasmodium falciparum, the causative agent of malaria, is critical for 
this organism's survival; the anti-Hsp90 drug geldanamycin is toxic to P. 
falciparum growth. We have solved the structure of the N-terminal ATP-binding 
domain of P. falciparum Hsp90, which contains a principal drug-binding pocket, 
in both apo and ADP-bound states at 2.3 A resolution. The structure shows that 
P. falciparum Hsp90 is highly similar to human Hsp90, and likely binds agents 
such as geldanamycin in an identical manner. Our results should aid in the 
structural understanding of Hsp90-drug interactions in P. falciparum, and 
provide a scaffold for future drug-discovery efforts.