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Crystal structure of a copper-transporting PIB-type ATPase

Author

Listed:
  • Pontus Gourdon

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C)

  • Xiang-Yu Liu

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
    State Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University)

  • Tina Skjørringe

    (Center for Applied Human Molecular Genetics, Kennedy Center, Gl. Landevej 7)

  • J. Preben Morth

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
    Present addresses: The Biotechnology Centre of Oslo and Centre for Molecular Medicine, Nordic EMBL Partnership, University of Oslo, 0318 Oslo, Norway (J.P.M.); Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158, USA (B.P.P.).)

  • Lisbeth Birk Møller

    (Center for Applied Human Molecular Genetics, Kennedy Center, Gl. Landevej 7)

  • Bjørn Panyella Pedersen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C
    Present addresses: The Biotechnology Centre of Oslo and Centre for Molecular Medicine, Nordic EMBL Partnership, University of Oslo, 0318 Oslo, Norway (J.P.M.); Department of Biochemistry and Biophysics, University of California at San Francisco, San Francisco, California 94158, USA (B.P.P.).)

  • Poul Nissen

    (Centre for Membrane Pumps in Cells and Disease—PUMPKIN, Danish National Research Foundation, Aarhus University, Gustav Wieds Vej 10C)

Abstract

Heavy-metal homeostasis and detoxification is crucial for cell viability. P-type ATPases of the class IB (PIB) are essential in these processes, actively extruding heavy metals from the cytoplasm of cells. Here we present the structure of a PIB-ATPase, a Legionella pneumophila CopA Cu+-ATPase, in a copper-free form, as determined by X-ray crystallography at 3.2 Å resolution. The structure indicates a three-stage copper transport pathway involving several conserved residues. A PIB-specific transmembrane helix kinks at a double-glycine motif displaying an amphipathic helix that lines a putative copper entry point at the intracellular interface. Comparisons to Ca2+-ATPase suggest an ATPase-coupled copper release mechanism from the binding sites in the membrane via an extracellular exit site. The structure also provides a framework to analyse missense mutations in the human ATP7A and ATP7B proteins associated with Menkes’ and Wilson’s diseases.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:nature:v:475:y:2011:i:7354:d:10.1038_nature10191
    DOI: 10.1038/nature10191
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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.
    2. 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.

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