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The structure and function of P5A-ATPases

Author

Listed:
  • Ping Li

    (Lund University)

  • Viktoria Bågenholm

    (University of Copenhagen)

  • Per Hägglund

    (University of Copenhagen)

  • Karin Lindkvist-Petersson

    (Lund University)

  • Kaituo Wang

    (University of Copenhagen
    Chinese Academy of Sciences)

  • Pontus Gourdon

    (Lund University
    University of Copenhagen)

Abstract

Endoplasmic reticulum (ER) membrane resident P5A-ATPases broadly affect protein biogenesis and quality control, and yet their molecular function remains debated. Here, we report cryo-EM structures of a P5A-ATPase, CtSpf1, covering multiple transport intermediates of the E1 → E1-ATP → E1P-ADP → E1P → E2P → E2.Pi → E2 → E1 cycle. In the E2P and E2.Pi states a cleft spans the entire membrane, holding a polypeptide cargo molecule. The cargo includes an ER luminal extension, pinpointed as the C-terminus in the E2.Pi state, which reenters the membrane in E2P. The E1 structure harbors a cytosol-facing cavity that is blocked by an insertion we refer to as the Plug-domain. The Plug-domain is nestled to key ATPase features and is displaced in the E1P-ADP and E1P states. Collectively, our findings are compatible with a broad range of proteins as cargo, with the P5A-ATPases serving a role in membrane removal of helices, although insertion/secretion cannot be excluded, as well as with a mechanistic role of the Plug-domain.

Suggested Citation

  • Ping Li & Viktoria Bågenholm & Per Hägglund & Karin Lindkvist-Petersson & Kaituo Wang & Pontus Gourdon, 2024. "The structure and function of P5A-ATPases," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-53757-6
    DOI: 10.1038/s41467-024-53757-6
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    References listed on IDEAS

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    1. Chikashi Toyoshima & Masayoshi Nakasako & Hiromi Nomura & Haruo Ogawa, 2000. "Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution," Nature, Nature, vol. 405(6787), pages 647-655, June.
    2. 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.
    3. 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.
    4. Ping Li & Kaituo Wang & Nina Salustros & Christina Grønberg & Pontus Gourdon, 2021. "Structure and transport mechanism of P5B-ATPases," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
    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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