High-resolution structures of malaria parasite actomyosin and actin filaments
Malaria is one of the most devastating infectious diseases in the world. The parasites causing malaria move by gliding, for which force is generated by an unusual actomyosin motor. We have determined high-resolution cryo-EM structures of the parasite actomyosin and actin filaments and a lower resolution reconstructions of the myosin light chains in the complex.
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In our article published today in the journal聽PLoS Pathogens, we聽present the first structure of the entire malaria parasite聽motor complex: actin 1 (PfAct1) and myosin A (PfMyoA) with its two light chains, essential light chain (ELC) and myosin light chain 1 (MLC1). We also report a high-resolution structure of filamentous聽PfAct1 that reveals new atomic details of the ATPase site, including a channel, which may provide an exit route for phosphate and explain why phosphate release is faster in聽PfAct1 compared to canonical actins.聽PfAct1 goes through no conformational changes upon聽PfMyoA binding. Our聽PfMyoA structure also superimposes with a recent crystal structure of聽PfMyoA alone and a lower-resolution cryo-EM structure of the MyoA-Act1 filament. However, there are small but important conformational changes at the interface. Our structures serve as a starting point for drug design against malaria, which is one of the most devastating infectious diseases.
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