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The complete structure of an activated open sodium channel

Author

Listed:
  • Altin Sula

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London)

  • Jennifer Booker

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London)

  • Leo C. T. Ng

    (Feinberg School of Medicine, Northwestern University)

  • Claire E. Naylor

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London)

  • Paul G. DeCaen

    (Feinberg School of Medicine, Northwestern University)

  • B. A. Wallace

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London)

Abstract

Voltage-gated sodium channels (Navs) play essential roles in excitable tissues, with their activation and opening resulting in the initial phase of the action potential. The cycling of Navs through open, closed and inactivated states, and their closely choreographed relationships with the activities of other ion channels lead to exquisite control of intracellular ion concentrations in both prokaryotes and eukaryotes. Here we present the 2.45 Å resolution crystal structure of the complete NavMs prokaryotic sodium channel in a fully open conformation. A canonical activated conformation of the voltage sensor S4 helix, an open selectivity filter leading to an open activation gate at the intracellular membrane surface and the intracellular C-terminal domain are visible in the structure. It includes a heretofore unseen interaction motif between W77 of S3, the S4–S5 interdomain linker, and the C-terminus, which is associated with regulation of opening and closing of the intracellular gate.

Suggested Citation

  • Altin Sula & Jennifer Booker & Leo C. T. Ng & Claire E. Naylor & Paul G. DeCaen & B. A. Wallace, 2017. "The complete structure of an activated open sodium channel," Nature Communications, Nature, vol. 8(1), pages 1-9, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14205
    DOI: 10.1038/ncomms14205
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    Cited by:

    1. Huiwen Chen & Zhanyi Xia & Jie Dong & Bo Huang & Jiangtao Zhang & Feng Zhou & Rui Yan & Yiqiang Shi & Jianke Gong & Juquan Jiang & Zhuo Huang & Daohua Jiang, 2024. "Structural mechanism of voltage-gated sodium channel slow inactivation," Nature Communications, Nature, vol. 15(1), pages 1-10, December.
    2. David Hollingworth & Frances Thomas & Dana A. Page & Mohamed A. Fouda & Raquel Lopez-Rios Castro & Altin Sula & Vitaliy B. Mykhaylyk & Geoff Kelly & Martin B. Ulmschneider & Peter C. Ruben & B. A. Wal, 2024. "Structural basis for the rescue of hyperexcitable cells by the amyotrophic lateral sclerosis drug Riluzole," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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