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Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels

Author

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  • C. Stock

    (Goethe University Frankfurt, Max-von-Laue-Straße 9)

  • L. Hielkema

    (University of Groningen)

  • I. Tascón

    (Goethe University Frankfurt, Max-von-Laue-Straße 9)

  • D. Wunnicke

    (Goethe University Frankfurt, Max-von-Laue-Straße 9)

  • G. T. Oostergetel

    (University of Groningen)

  • M. Azkargorta

    (Proteomics Platform, CIC bioGUNE, CIBERehd, ProteoRed-ISCIII, Bizkaia Science and Technology Park)

  • C. Paulino

    (University of Groningen)

  • I. Hänelt

    (Goethe University Frankfurt, Max-von-Laue-Straße 9)

Abstract

P-type ATPases ubiquitously pump cations across biological membranes to maintain vital ion gradients. Among those, the chimeric K+ uptake system KdpFABC is unique. While ATP hydrolysis is accomplished by the P-type ATPase subunit KdpB, K+ has been assumed to be transported by the channel-like subunit KdpA. A first crystal structure uncovered its overall topology, suggesting such a spatial separation of energizing and transporting units. Here, we report two cryo-EM structures of the 157 kDa, asymmetric KdpFABC complex at 3.7 Å and 4.0 Å resolution in an E1 and an E2 state, respectively. Unexpectedly, the structures suggest a translocation pathway through two half-channels along KdpA and KdpB, uniting the alternating-access mechanism of actively pumping P-type ATPases with the high affinity and selectivity of K+ channels. This way, KdpFABC would function as a true chimeric complex, synergizing the best features of otherwise separately evolved transport mechanisms.

Suggested Citation

  • C. Stock & L. Hielkema & I. Tascón & D. Wunnicke & G. T. Oostergetel & M. Azkargorta & C. Paulino & I. Hänelt, 2018. "Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two inter-subunit half-channels," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07319-2
    DOI: 10.1038/s41467-018-07319-2
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    Cited by:

    1. Nina Salustros & Christina Grønberg & Nisansala S. Abeyrathna & Pin Lyu & Fredrik Orädd & Kaituo Wang & Magnus Andersson & Gabriele Meloni & Pontus Gourdon, 2022. "Structural basis of ion uptake in copper-transporting P1B-type ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
    2. Jakob M. Silberberg & Sophie Ketter & Paul J. N. Böhm & Kristin Jordan & Marcel Wittenberg & Julia Grass & Inga Hänelt, 2024. "KdpD is a tandem serine histidine kinase that controls K+ pump KdpFABC transcriptionally and post-translationally," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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