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

Balasundaresan Dhakshnamoorthy, Ahmed Rohaim, Huan Rui, Lydia Blachowicz and Benoît Roux ()
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Balasundaresan Dhakshnamoorthy: The University of Chicago
Ahmed Rohaim: The University of Chicago
Huan Rui: The University of Chicago
Lydia Blachowicz: The University of Chicago
Benoît Roux: The University of Chicago

Nature Communications, 2016, vol. 7, issue 1, 1-11

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms12753

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