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


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 Ca(2+) concentration. In the crystal structure, the selectivity filter adopts a novel conformation with Ca(2+) 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 Ca(2+) 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.

SUBMITTER: Dhakshnamoorthy B 

PROVIDER: S-EPMC5052707 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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

Dhakshnamoorthy Balasundaresan B   Rohaim Ahmed A   Rui Huan H   Blachowicz Lydia L   Roux Benoît B  

Nature communications 20160928


The selectivity filter is an essential functional element of K<sup>+</sup> 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 Ca<sup>2+</sup> con  ...[more]

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