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Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing

Author

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  • Emily C. McCusker

    (Institute of Structural and Molecular Biology, Birkbeck College, University of London
    Present address: Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California 94158-2517, USA)

  • Claire Bagnéris

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

  • Claire E. Naylor

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

  • Ambrose R. Cole

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

  • Nazzareno D'Avanzo

    (Excitability Diseases, Washington University School of Medicine
    Present address: Department of Physiology and GEPROM, Université de Montréal, Montréal, Québec, Canada H3C 3J7)

  • Colin G. Nichols

    (Excitability Diseases, Washington University School of Medicine)

  • B.A. Wallace

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

Abstract

Sodium-gated ion channels open and close in response to the flow of ions. Here, McCusker et al.report the open structure of a sodium-gated ion channel pore from a bacterial homologue, and show, by comparison with the closed structure, that the movement of a C-terminal helix is sufficient to open the channel.

Suggested Citation

  • Emily C. McCusker & Claire Bagnéris & Claire E. Naylor & Ambrose R. Cole & Nazzareno D'Avanzo & Colin G. Nichols & B.A. Wallace, 2012. "Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing," Nature Communications, Nature, vol. 3(1), pages 1-8, January.
    • Handle: RePEc:nat:natcom:v:3:y:2012:i:1:d:10.1038_ncomms2077
    DOI: 10.1038/ncomms2077
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