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  • 1.
    Delemotte, Lucie
    KTH, School of Engineering Sciences (SCI), Applied Physics, Biophysics.
    Outlining the proton-conduction pathway in otopetrin channels2019In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 26, no 7, p. 528-530Article in journal (Other academic)
  • 2.
    Fernandez-Marino, Ana I.
    et al.
    Univ Wisconsin, SMPH, Dept Neurosci, Madison, WI 53706 USA.;NINDS, Mol Physiol & Biophys Sect, Porter Neurosci Res Ctr, NIH, Bldg 36,Rm 4D04, Bethesda, MD 20892 USA..
    Harpole, Tyler J.
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Oelstrom, Kevin
    Univ Wisconsin, SMPH, Dept Neurosci, Madison, WI 53706 USA.;Cellular Dynam Int Inc, Madison, WI USA..
    Delemotte, Lucie
    KTH, School of Engineering Sciences (SCI), Applied Physics. KTH, Centres, Science for Life Laboratory, SciLifeLab.
    Chanda, Baron
    Univ Wisconsin, SMPH, Dept Neurosci, Madison, WI 53706 USA.;Univ Wisconsin, SMPH, Dept Biomol Chem, Madison, WI 53706 USA..
    Gating interaction maps reveal a noncanonical electromechanical coupling mode in the Shaker K+ channel2018In: Nature Structural & Molecular Biology, ISSN 1545-9993, E-ISSN 1545-9985, Vol. 25, no 4, p. 320-326Article in journal (Refereed)
    Abstract [en]

    Membrane potential regulates the activity of voltage-dependent ion channels via specialized voltage-sensing modules, but the mechanisms involved in coupling voltage-sensor movement to pore opening remain unclear owing to a lack of resting state structures and robust methods to identify allosteric pathways. Here, using a newly developed interaction-energy analysis, we probe the interfaces of the voltage-sensing and pore modules in the Drosophila Shaker K+ channel. Our measurements reveal unexpectedly strong equilibrium gating interactions between contacts at the S4 and S5 helices in addition to those between S6 and the S4-S5 linker. Network analysis of MD trajectories shows that the voltage-sensor and pore motions are linked by two distinct pathways: a canonical pathway through the S4-S5 linker and a hitherto unknown pathway akin to rack-and-pinion coupling involving the S4 and S5 helices. Our findings highlight the central role of the S5 helix in electromechanical transduction in the voltage-gated ion channel (VGIC) superfamily.

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