9N10

P. falciparum P-type ATPase, PfATP4

Summary for 9N10

• Entry DOI: 10.2210/pdb9n10/pdb
• EMDB information: 48801
• Descriptor: Non-SERCA-type Ca2+ -transporting P-ATPase, PfATP4 Binding Protein (PfABP) (2 entities in total)
• Functional Keywords: p-type atpase, membrane protein
• Biological source: Plasmodium falciparum Dd2; More
• Total number of polymer chains: 2
• Total formula weight: 161896.74

Authors

Haile, M.T.,Zhen, J.,Ho, C. (deposition date: 2025-01-24, release date: 2025-10-15, Last modification date: 2025-11-05)

Primary citation

Haile, M.T.,Shukla, A.,Zhen, J.,Mather, M.W.,Bhatnagar, S.,Morrisey, J.M.,Zhang, Z.,Vaidya, A.B.,Ho, C.M.
Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator.
Nat Commun, 16:9092-9092, 2025

PubMed Abstract: 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.

PubMed: 41115914
DOI: 10.1038/s41467-025-64815-y

Experimental method

ELECTRON MICROSCOPY (3.8 Å)