ArticleProceedings of the National Academy of Sciences of the United States of America2010
The activated state of a sodium channel voltage sensor in a membrane environment.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed.
- Preorganized Electric Fields in Voltage-Gated Sodium Channels.Chembiochem : a European journal of chemical biology · 2025Article
- Modulation of Kv Channel Gating by Light-Controlled Membrane Thickness.Biomolecules · 2025Article
- Electrosome assembly: Structural insights from high voltage-activated calcium channel (CaV)-chaperone interactions.Biochemical Society transactions · 2025Review
- Characterization of two pathological gating-charge substitutions in Cav1.4 L-type calcium channels.Channels (Austin, Tex.) · 2023Article
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.Nature structural & molecular biology · 2022Article
- Article
- Charge substitutions at the voltage-sensing module of domain III enhance actions of site-3 and site-4 toxins on an insect sodium channel.Insect biochemistry and molecular biology · 2021Article
- Roles for Countercharge in the Voltage Sensor Domain of Ion Channels.Frontiers in pharmacology · 2020Review
- Site Directed Spin Labeling and EPR Spectroscopic Studies of Pentameric Ligand-Gated Ion Channels.Journal of visualized experiments : JoVE · 2016Article
- Resting state of the human proton channel dimer in a lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Structural Refinement of Proteins by Restrained Molecular Dynamics Simulations with Non-interacting Molecular Fragments.PLoS computational biology · 2015Article
- Bacterial voltage-gated sodium channels (BacNa(V)s) from the soil, sea, and salt lakes enlighten molecular mechanisms of electrical signaling and pharmacology in the brain and heart.Journal of molecular biology · 2015Review
- EPR Studies of Gating Mechanisms in Ion Channels.Methods in enzymology · 2015Review
- Tracking S4 movement by gating pore currents in the bacterial sodium channel NaChBac.The Journal of general physiology · 2014Article
- Structural basis of lipid-driven conformational transitions in the KvAP voltage-sensing domain.Nature structural & molecular biology · 2014Article
- Sensing charges of the Ciona intestinalis voltage-sensing phosphatase.The Journal of general physiology · 2013Article
- Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Neuron · 2013Review
- Structural changes in the mitochondrial Tim23 channel are coupled to the proton-motive force.Nature structural & molecular biology · 2013Article
- Energetic role of the paddle motif in voltage gating of Shaker K(+) channels.Nature structural & molecular biology · 2013Article
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5 authors.
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Abstract
Direct structural insights on the fundamental mechanisms of permeation, selectivity, and gating remain unavailable for the Na(+) and Ca(2+) channel families. Here, we report the spectroscopic structural characterization of the isolated Voltage-Sensor Domain (VSD) of the prokaryotic Na(+) channel NaChBac in a lipid bilayer. Site-directed spin-labeling and EPR spectroscopy were carried out for 118 mutants covering all of the VSD. EPR environmental data were used to unambiguously assign the secondary structure elements, define membrane insertion limits, and evaluate the activated conformation of the isolated-VSD in the membrane using restrain-driven molecular dynamics simulations. The overall three-dimensional fold of the NaChBac-VSD closely mirrors those seen in KvAP, Kv1.2, Kv1.2-2.1 chimera, and MlotiK1. However, in comparison to the membrane-embedded KvAP-VSD, the structural dynamics of the NaChBac-VSD reveals a much tighter helix packing, with subtle differences in the local environment of the gating charges and their interaction with the rest of the protein. Using cell complementation assays we show that the NaChBac-VSD can provide a conduit to the transport of ions in the resting or "down" conformation, a feature consistent with our EPR water accessibility measurements in the activated or "up" conformation. These results suggest that the overall architecture of VSD's is remarkably conserved among K(+) and Na(+) channels and that pathways for gating-pore currents may be intrinsic to most voltage-sensors. Cell complementation assays also provide information about the putative location of the gating charges in the "down/resting" state and hence a glimpse of the extent of conformational changes during activation.
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