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• W2524936633 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." @default.
• W2524936633 created "2016-10-07" @default.
• W2524936633 creator A5011596226 @default.
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• W2524936633 date "2016-09-28" @default.
• W2524936633 modified "2023-10-16" @default.
• W2524936633 title "Structural and functional characterization of a calcium-activated cation channel from Tsukamurella paurometabola" @default.
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• W2524936633 doi "https://doi.org/10.1038/ncomms12753" @default.
• W2524936633 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5052707" @default.
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• W2524936633 hasPublicationYear "2016" @default.
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