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Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola

Author

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  • Balasundaresan Dhakshnamoorthy

    (The University of Chicago)

  • Ahmed Rohaim

    (The University of Chicago
    Faculty of Science, Cairo University)

  • Huan Rui

    (The University of Chicago)

  • Lydia Blachowicz

    (The University of Chicago)

  • Benoît Roux

    (The University of Chicago)

Abstract

The selectivity filter is an essential functional element of K+ channels that is highly conserved both in terms of its primary sequence and its three-dimensional structure. Here, we investigate the properties of an ion channel from the Gram-positive bacterium Tsukamurella paurometabola with a selectivity filter formed by an uncommon proline-rich sequence. Electrophysiological recordings show that it is a non-selective cation channel and that its activity depends on Ca2+ concentration. In the crystal structure, the selectivity filter adopts a novel conformation with Ca2+ ions bound within the filter near the pore helix where they are coordinated by backbone oxygen atoms, a recurrent motif found in multiple proteins. The binding of Ca2+ ion in the selectivity filter controls the widening of the pore as shown in crystal structures and in molecular dynamics simulations. The structural, functional and computational data provide a characterization of this calcium-gated cationic channel.

Suggested Citation

  • Balasundaresan Dhakshnamoorthy & Ahmed Rohaim & Huan Rui & Lydia Blachowicz & Benoît Roux, 2016. "Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola," Nature Communications, Nature, vol. 7(1), pages 1-11, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12753
    DOI: 10.1038/ncomms12753
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