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TitleEndogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 9092, Year 2025
Publish dateOct 20, 2025
AuthorsMeseret T Haile / Anurag Shukla / James Zhen / Michael W Mather / Suyash Bhatnagar / Joanne M Morrisey / Zhening Zhang / Akhil B Vaidya / Chi-Min Ho /
PubMed AbstractThe 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 ...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 Å 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 an unexplored avenue for designing PfATP4 inhibitors.
External linksNat Commun / PubMed:41115914 / PubMed Central
MethodsEM (single particle)
Resolution3.8 Å
Structure data

EMDB-48800: P. falciparum P-type ATPase, PfATP4 re-centered in the P-domain
Method: EM (single particle) / Resolution: 3.8 Å

48801

9n10

EMDB-48801, PDB-9n10:
P. falciparum P-type ATPase, PfATP4
Method: EM (single particle) / Resolution: 3.8 Å

Source
  • plasmodium falciparum dd2 (eukaryote)
KeywordsMEMBRANE PROTEIN / P-type ATPase

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