Endogenous structure of antimalarial target PfATP4 reveals new class of apicomplexan P-type ATPase modulators
Haile, M. T.; Shukla, A.; Zhen, J.; Mather, M. W.; Bhatnagar, S.; Zhang, Z.; Vaidya, A. B.; Ho, C.-M.
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The Plasmodium falciparum sodium efflux pump PfATP4 is a leading antimalarial target, but suffers from a lack of high-resolution structural information needed to identify functionally important features in conserved regions and guide rational design of next generation inhibitors. Here, we determine a 3.7[A] cryoEM structure of PfATP4 purified from CRISPR-engineered P. falciparum parasites, revealing a previously unknown, apicomplexan-specific binding partner, PfABP, which forms a conserved, likely modulatory interaction with PfATP4. The discovery of PfABP presents a new avenue for designing novel PfATP4 inhibitors.
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