2024
DOI: 10.1038/s44319-023-00037-x
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Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases

Jannik Strauss,
Craig Wilkinson,
Keni Vidilaseris
et al.

Abstract: Membrane-bound pyrophosphatases (M-PPases) are homodimeric primary ion pumps that couple the transport of Na+- and/or H+ across membranes to the hydrolysis of pyrophosphate. Their role in the virulence of protist pathogens like Plasmodium falciparum makes them an intriguing target for structural and functional studies. Here, we show the first structure of a K+-independent M-PPase, asymmetric and time-dependent substrate binding in time-resolved structures of a K+-dependent M-PPase and demonstrate pumping-befor… Show more

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