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Structural basis of ion uptake in copper-transporting P1B-type ATPases

Author

Listed:
  • Nina Salustros

    (Copenhagen University)

  • Christina Grønberg

    (Copenhagen University)

  • Nisansala S. Abeyrathna

    (The University of Texas at Dallas)

  • Pin Lyu

    (Copenhagen University
    University of Copenhagen)

  • Fredrik Orädd

    (Umeå University)

  • Kaituo Wang

    (Copenhagen University)

  • Magnus Andersson

    (Umeå University)

  • Gabriele Meloni

    (The University of Texas at Dallas)

  • Pontus Gourdon

    (Copenhagen University
    Lund University)

Abstract

Copper is essential for living cells, yet toxic at elevated concentrations. Class 1B P-type (P1B-) ATPases are present in all kingdoms of life, facilitating cellular export of transition metals including copper. P-type ATPases follow an alternating access mechanism, with inward-facing E1 and outward-facing E2 conformations. Nevertheless, no structural information on E1 states is available for P1B-ATPases, hampering mechanistic understanding. Here, we present structures that reach 2.7 Å resolution of a copper-specific P1B-ATPase in an E1 conformation, with complementing data and analyses. Our efforts reveal a domain arrangement that generates space for interaction with ion donating chaperones, and suggest a direct Cu+ transfer to the transmembrane core. A methionine serves a key role by assisting the release of the chaperone-bound ion and forming a cargo entry site together with the cysteines of the CPC signature motif. Collectively, the findings provide insights into P1B-mediated transport, likely applicable also to human P1B-members.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32751-w
    DOI: 10.1038/s41467-022-32751-w
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    References listed on IDEAS

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    1. Pontus Gourdon & Xiang-Yu Liu & Tina Skjørringe & J. Preben Morth & Lisbeth Birk Møller & Bjørn Panyella Pedersen & Poul Nissen, 2011. "Crystal structure of a copper-transporting PIB-type ATPase," Nature, Nature, vol. 475(7354), pages 59-64, July.
    2. Chikashi Toyoshima & Hiromi Nomura & Takeo Tsuda, 2004. "Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues," Nature, Nature, vol. 432(7015), pages 361-368, November.
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    4. Kaituo Wang & Oleg Sitsel & Gabriele Meloni & Henriette Elisabeth Autzen & Magnus Andersson & Tetyana Klymchuk & Anna Marie Nielsen & Douglas C. Rees & Poul Nissen & Pontus Gourdon, 2014. "Structure and mechanism of Zn2+-transporting P-type ATPases," Nature, Nature, vol. 514(7523), pages 518-522, October.
    5. Anne-Marie L. Winther & Maike Bublitz & Jesper L. Karlsen & Jesper V. Møller & John B. Hansen & Poul Nissen & Morten J. Buch-Pedersen, 2013. "The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm," Nature, Nature, vol. 495(7440), pages 265-269, March.
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    Cited by:

    1. Zongxin Guo & Fredrik Orädd & Viktoria Bågenholm & Christina Grønberg & Jian Feng Ma & Peter Ott & Yong Wang & Magnus Andersson & Per Amstrup Pedersen & Kaituo Wang & Pontus Gourdon, 2024. "Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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