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Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase

Author

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  • Matteo Allegretti

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

  • Niklas Klusch

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

  • Deryck J. Mills

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

  • Janet Vonck

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

  • Werner Kühlbrandt

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

  • Karen M. Davies

    (Max Planck Institute of Biophysics, Max-von-Laue-Strasse 3, 60438 Frankfurt am Main, Germany)

Abstract

Electron cryomicroscopy of a complete mitochondrial ATP-synthase dimer reveals the elusive structure of the essential a-subunit.

Suggested Citation

  • Matteo Allegretti & Niklas Klusch & Deryck J. Mills & Janet Vonck & Werner Kühlbrandt & Karen M. Davies, 2015. "Horizontal membrane-intrinsic α-helices in the stator a-subunit of an F-type ATP synthase," Nature, Nature, vol. 521(7551), pages 237-240, May.
    • Handle: RePEc:nat:nature:v:521:y:2015:i:7551:d:10.1038_nature14185
    DOI: 10.1038/nature14185
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    Cited by:

    1. J. Kishikawa & A. Nakanishi & A. Nakano & S. Saeki & A. Furuta & T. Kato & K. Mistuoka & K. Yokoyama, 2022. "Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases," Nature Communications, Nature, vol. 13(1), pages 1-11, December.

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