Journal Article

PUBDB-2024-01735

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Functional and structural asymmetry suggest a unifying principle for catalysis in membrane-bound pyrophosphatases

Strauss, J. ; Wilkinson, C. ; Vidilaseris, K. ; de Castro Ribeiro, O. M. ; Liu, J. ; Hillier, J. ; Wichert, M. ; Malinen, A. M. ; Gehl, B. ; Jeuken, L. J. ; Pearson, A. R. ; Goldman, A. (Corresponding author)

2024
Wiley Hoboken, NJ [u.a.]

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Please use a persistent id in citations: doi:10.1038/s44319-023-00037-x  doi:10.3204/PUBDB-2024-01735

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-before-hydrolysis by electrometric studies. We suggest how key residues in helix 12, 13, and the exit channel loops affect ion selectivity and K+-activation due to a complex interplay of residues that are involved in subunit-subunit communication. Our findings not only explain ion selectivity in M-PPases but also why they display half-of-the-sites reactivity. Based on this, we propose, for the first time, a unified model for ion-pumping, hydrolysis, and energy coupling in all M-PPases, including those that pump both Na+ and H+.

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Contributing Institute(s):

1. EMBL-User (EMBL-User)

Research Program(s):

1. 6G3 - PETRA III (DESY) (POF4-6G3) (POF4-6G3)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2024

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Database coverage:
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