ArticleJournal of molecular biology2014
Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.
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Who cites it
86 citing papers in PubMed.
- Structure-function analysis of the lithium-ion selectivity of the voltage-gated sodium channel.The Journal of general physiology · 2026Article
- Deciphering CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Incorporating the thermodynamic effects of temperature and pressure on modeling neuronal gating kinetics.PloS one · 2025Article
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- Honeybee CaV4 has distinct permeation, inactivation, and pharmacology from homologous NaV channels.The Journal of general physiology · 2024Article
- Structural mechanism of voltage-gated sodium channel slow inactivation.Nature communications · 2024Article
- Asymmetric Lipid Bilayers and Potassium Channels Embedded Therein in the Contact Bubble Bilayer.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Ion channel selectivity through ion-modulated changes of selectivity filter pProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular Dynamics Simulations of Ion Permeation in Human Voltage-Gated Sodium Channels.Journal of chemical theory and computation · 2023Article
- Article
- The unique structural characteristics of the Kir 7.1 inward rectifier potassium channel: a novel player in energy homeostasis control.American journal of physiology. Cell physiology · 2023Review
- An α-π transition in S6 shapes the conformational cycle of the bacterial sodium channel NavAb.The Journal of general physiology · 2023Article
- Quaternary structure independent folding of voltage-gated ion channel pore domain subunits.Nature structural & molecular biology · 2022Article
- Differential effects of modified batrachotoxins on voltage-gated sodium channel fast and slow inactivation.Cell chemical biology · 2022Article
- The T1-tetramerisation domain of Kv1.2 rescues expression and preserves function of a truncated NaChBac sodium channel.FEBS letters · 2022Article
- An open state of a voltage-gated sodium channel involving a π-helix and conserved pore-facing asparagine.Biophysical journal · 2022Article
- Determinants of conductance of a bacterial voltage-gated sodium channel.Biophysical journal · 2021Article
- Review
- Structural Basis for High-Affinity Trapping of the NaMolecular cell · 2021Article
- Structural basis for voltage-sensor trapping of the cardiac sodium channel by a deathstalker scorpion toxin.Nature communications · 2021Article
26 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Voltage-gated sodium channels (NaVs) are central elements of cellular excitation. Notwithstanding advances from recent bacterial NaV (BacNaV) structures, key questions about gating and ion selectivity remain. Here, we present a closed conformation of NaVAe1p, a pore-only BacNaV derived from NaVAe1, a BacNaV from the arsenite oxidizer Alkalilimnicola ehrlichei found in Mono Lake, California, that provides insight into both fundamental properties. The structure reveals a pore domain in which the pore-lining S6 helix connects to a helical cytoplasmic tail. Electrophysiological studies of full-length BacNaVs show that two elements defined by the NaVAe1p structure, an S6 activation gate position and the cytoplasmic tail "neck", are central to BacNaV gating. The structure also reveals the selectivity filter ion entry site, termed the "outer ion" site. Comparison with mammalian voltage-gated calcium channel (CaV) selectivity filters, together with functional studies, shows that this site forms a previously unknown determinant of CaV high-affinity calcium binding. Our findings underscore commonalities between BacNaVs and eukaryotic voltage-gated channels and provide a framework for understanding gating and ion permeation in this superfamily.
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