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The gating ring-forming RCK domain regulates channel gating in response to various cellular chemical stimuli in eukaryotic Slo channel families and the majority of ligand-gated prokaryotic K(+) channels and transporters. Here we present structural and functional studies of a dual RCK-containing, multi-ligand gated K(+) channel from Geobacter sulfurreducens, named GsuK. We demonstrate that ADP and NAD(+) activate the GsuK channel, whereas Ca(2+) serves as an allosteric inhibitor. Multiple crystal structures elucidate the structural basis of multi-ligand gating in GsuK, and also reveal a unique ion conduction pore with segmented inner helices. Structural comparison leads us to propose a novel pore opening mechanics that is distinct from other K(+) channels.DOI:http://dx.doi.org/10.7554/eLife.00184.001.

Original publication

DOI

10.7554/elife.00184

Type

Journal article

Journal

eLife

Publication Date

12/2012

Volume

1

Addresses

Department of Physiology , University of Texas Southwestern Medical Center , Dallas , United States.

Keywords

Geobacter, Escherichia coli, Calcium, NAD, Bacterial Proteins, Potassium Channels, Recombinant Proteins, Adenosine Diphosphate, Ligands, Crystallography, X-Ray, Sequence Alignment, Ion Channel Gating, Gene Expression, Allosteric Regulation, Amino Acid Sequence, Protein Structure, Secondary, Protein Structure, Tertiary, Models, Molecular, Molecular Sequence Data, Ligand-Gated Ion Channels