ArticleBiophysical journal2014
Effects of the protonation state of the EEEE motif of a bacterial Na(+)-channel on conduction and pore structure.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The chemistry of electrical signaling in sodium channels from bacteria and beyond.Cell chemical biology · 2024Review
- Ion channel selectivity through ion-modulated changes of selectivity filter pProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Determinants of conductance of a bacterial voltage-gated sodium channel.Biophysical journal · 2021Article
- Application of a Statistical and Linear Response Theory to Multi-Ion NaEntropy (Basel, Switzerland) · 2021Article
- The insights into calcium ion selectivity provided by ancestral prokaryotic ion channels.Biophysics and physicobiology · 2021Article
- Changes in Ion Selectivity Following the Asymmetrical Addition of Charge to the Selectivity Filter of Bacterial Sodium Channels.Entropy (Basel, Switzerland) · 2020Article
- Bases of Bacterial Sodium Channel Selectivity Among Organic Cations.Scientific reports · 2019Article
- Role of the Interaction Motif in Maintaining the Open Gate of an Open Sodium Channel.Biophysical journal · 2018Article
- Molecular Dynamics of Ion Conduction through the Selectivity Filter of the NaThe journal of physical chemistry. B · 2018Article
- Selective ion permeation involves complexation with carboxylates and lysine in a model human sodium channel.PLoS computational biology · 2018Article
- Molecular basis of ion permeability in a voltage-gated sodium channel.The EMBO journal · 2016Article
- Article
- Theoretical and simulation studies on voltage-gated sodium channels.Protein & cell · 2015Review
- Article
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3 authors.
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Abstract
A distinctive feature of prokaryotic Na(+)-channels is the presence of four glutamate residues in their selectivity filter. In this study, how the structure of the selectivity filter, and the free-energy profile of permeating Na(+) ions are altered by the protonation state of Glu177 are analyzed. It was found that protonation of a single glutamate residue was enough to modify the conformation of the selectivity filter and its conduction properties. Molecular dynamics simulations revealed that Glu177 residues may adopt two conformations, with the side chain directed toward the extracellular entrance of the channel or the intracellular cavity. The likelihood of the inwardly directed arrangement increases when Glu177 residues are protonated. The presence of one glutamate residue with its chain directed toward the intracellular cavity increases the energy barrier for translocation of Na(+) ions. These higher-energy barriers preclude Na(+) ions to permeate the selectivity filter of prokaryotic Na(+)-channels when one or more Glu177 residues are protonated.
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