ArticleThe Journal of general physiology2013
Molecular interactions involved in proton-dependent gating in KcsA potassium channels.
Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 24 citations in OpenAlex.
- Cooperativity in regulation of membrane protein function: phenomenological analysis of the effects of pH and phospholipids.Biophysical reviews · 2023Review
- Article
- Tetraoctylammonium, a Long Chain Quaternary Ammonium Blocker, Promotes a Noncollapsed, Resting-Like Inactivated State in KcsA.International journal of molecular sciences · 2021Article
- Probing allosteric coupling in a constitutively open mutant of the ion channel KcsA using solid-state NMR.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
- Identifying coupled clusters of allostery participants through chemical shift perturbations.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Article
- Selective exclusion and selective binding both contribute to ion selectivity in KcsA, a model potassium channel.The Journal of biological chemistry · 2017Article
- Transmembrane allosteric energetics characterization for strong coupling between proton and potassium ion binding in the KcsA channel.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conformational dynamics and role of the acidic pocket in ASIC pH-dependent gating.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Conformational heterogeneity in closed and open states of the KcsA potassium channel in lipid bicelles.The Journal of general physiology · 2016Article
- Channel function reconstitution and re-animation: a single-channel strategy in the postcrystal age.The Journal of physiology · 2015Review
- Structural requirements in the transmembrane domain of GLIC revealed by incorporation of noncanonical histidine analogs.Chemistry & biology · 2014Article
- A KcsA/MloK1 chimeric ion channel has lipid-dependent ligand-binding energetics.The Journal of biological chemistry · 2014Article
- Inactivation in the potassium channel KcsA.Journal of structural biology: XArticle
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
Abstract
The bacterial potassium channel KcsA is gated open by the binding of protons to amino acids on the intracellular side of the channel. We have identified, via channel mutagenesis and x-ray crystallography, two pH-sensing amino acids and a set of nearby residues involved in molecular interactions that influence gating. We found that the minimal mutation of one histidine (H25) and one glutamate (E118) near the cytoplasmic gate completely abolished pH-dependent gating. Mutation of nearby residues either alone or in pairs altered the channel's response to pH. In addition, mutations of certain pairs of residues dramatically increased the energy barriers between the closed and open states. We proposed a Monod-Wyman-Changeux model for proton binding and pH-dependent gating in KcsA, where H25 is a "strong" sensor displaying a large shift in pKa between closed and open states, and E118 is a "weak" pH sensor. Modifying model parameters that are involved in either the intrinsic gating equilibrium or the pKa values of the pH-sensing residues was sufficient to capture the effects of all mutations.
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