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 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

SUBMITTER: Dhakshnamoorthy B 

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

REPOSITORIES: biostudies-literature