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

Emily C. McCusker, Claire Bagnéris, Claire E. Naylor, Ambrose R. Cole, Nazzareno D'Avanzo, Colin G. Nichols and B.A. Wallace ()
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Emily C. McCusker: Institute of Structural and Molecular Biology, Birkbeck College, University of London
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
Colin G. Nichols: Excitability Diseases, Washington University School of Medicine
B.A. Wallace: Institute of Structural and Molecular Biology, Birkbeck College, University of London

Nature Communications, 2012, vol. 3, issue 1, 1-8

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.

Date: 2012
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DOI: 10.1038/ncomms2077

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