ArticleScientific reports2013
The open gate structure of the membrane-embedded KcsA potassium channel viewed from the cytoplasmic side.
Article in Scientific reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Cardiolipin binding enhances KcsA channel gating via both its specific and dianion-monoanion interchangeable sites.iScience · 2023Article
- Computation of topographic and three-dimensional atomic force microscopy images of biopolymers by calculating forces.Biophysical reviews · 2023Review
- Article
- Mechanisms underlying drug-mediated regulation of membrane protein function.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Conductance selectivity of NaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Queueing arrival and release mechanism for KThe journal of physiological sciences : JPS · 2019Article
- Constitutive boost of a KProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Coupling neutron reflectivity with cell-free protein synthesis to probe membrane protein structure in supported bilayers.Scientific reports · 2017Article
- Channel function reconstitution and re-animation: a single-channel strategy in the postcrystal age.The Journal of physiology · 2015Review
- Atomic force microscopy of asymmetric membranes from turtle erythrocytes.Molecules and cells · 2014Article
- Multiparametric high-resolution imaging of native proteins by force-distance curve-based AFM.Nature protocols · 2014Article
- Regulation of ion channel function by the host lipid bilayer examined by a stopped-flow spectrofluorometric assay.Biophysical journal · 2014Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Crystallographic studies of channel proteins have provided insight into the molecular mechanisms of ion channels, even though these structures are obtained in the absence of the membrane and some structural portions have remained unsolved. Here we report the gating structure of the membrane-embedded KcsA potassium channel using atomic force microscopy (AFM). The activation gate of the KcsA channel is located on the intracellular side, and the cytoplasmic domain was truncated to clear the view of this location. Once opened, the individual subunits in the tetramer were resolved with the pore open at the center. Furthermore, AFM was able to capture the previously unsolved bulge helix at the entrance. A molecular dynamics simulation revealed that the bulge helices fluctuated dramatically at the open entryway. This dynamic behavior was observed as vigorous open-channel noise in the single-channel current recordings. The role of the bulge helices in the open gate structure is discussed.
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