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2016 - Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola

icon pap  Port-a-Patch and   icon vpp   Vesicle Prep Pro publication in Nature Communications (2016)

Authors:
Dhakshnamoorthy B., Rohaim A., Rui H., Blachowicz L., Roux B.

 

Journal:
Nature Communications (2016) 7:12753


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.


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