ArticleProceedings of the National Academy of Sciences of the United States of America2006
Distance measurements reveal a common topology of prokaryotic voltage-gated ion channels in the lipid bilayer.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Small molecule modulation of voltage gated sodium channels.Current opinion in structural biology · 2017Review
- β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Mechanistic Insights into the Modulation of Voltage-Gated Ion Channels by Inhalational Anesthetics.Biophysical journal · 2015Review
- Application of fluorescence resonance energy transfer in protein studies.Journal of molecular structure · 2014Article
- A limited 4 Å radial displacement of the S4-S5 linker is sufficient for internal gate closing in Kv channels.The Journal of biological chemistry · 2012Article
- Nano-positioning system for structural analysis of functional homomeric proteins in multiple conformations.Structure (London, England : 1993) · 2012Article
- Hinge-bending motions in the pore domain of a bacterial voltage-gated sodium channel.Biochimica et biophysica acta · 2012Article
- Coupling between the voltage-sensing and pore domains in a voltage-gated potassium channel.Biochimica et biophysica acta · 2012Article
- In vitro folding of KvAP, a voltage-gated K+ channel.Biochemistry · 2011Article
- Paul F. Cranefield Award to Rikard Blunck.The Journal of general physiology · 2011Article
- NaChBac: the long lost sodium channel ancestor.Biochemistry · 2011Article
- Arrangement and mobility of the voltage sensor domain in prokaryotic voltage-gated sodium channels.The Journal of biological chemistry · 2011Article
- Multi-scale electrophysiology modeling: from atom to organ.The Journal of general physiology · 2010Article
- The activated state of a sodium channel voltage sensor in a membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Fluorescence detection of the movement of single KcsA subunits reveals cooperativity.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Models of voltage-dependent conformational changes in NaChBac channels.Biophysical journal · 2008Article
- Models of the structure and gating mechanisms of the pore domain of the NaChBac ion channel.Biophysical journal · 2008Article
- Article
- The structure of the lipid-embedded potassium channel voltage sensor determined by double-electron-electron resonance spectroscopy.Protein science : a publication of the Protein Society · 2008Article
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7 authors.
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Abstract
Voltage-dependent ion channels are fundamental to the physiology of excitable cells because they underlie the generation and propagation of the action potential and excitation-contraction coupling. To understand how ion channels work, it is important to determine their structures in different conformations in a membrane environment. The validity of the crystal structure for the prokaryotic K(+) channel, K(V)AP, has been questioned based on discrepancies with biophysical data from functional eukaryotic channels, underlining the need for independent structural data under native conditions. We investigated the structural organization of two prokaryotic voltage-gated channels, NaChBac and K(V)AP, in liposomes by using luminescence resonance energy transfer. We describe here a transmembrane packing representation of the voltage sensor and pore domains of the prokaryotic Na channel, NaChBac. We find that NaChBac and K(V)AP share a common arrangement in which the structures of the Na and K selective pores and voltage-sensor domains are conserved. The packing arrangement of the voltage-sensing region as determined by luminescence resonance energy transfer differs significantly from that of the K(V)AP crystal structure, but resembles that of the eukaryotic K(V)1.2 crystal structure. However, the voltage-sensor domain in prokaryotic channels is closer to the pore domain than in the K(V)1.2 structure. Our results indicate that prokaryotic and eukaryotic channels that share similar functional properties have similar helix arrangements, with differences arising likely from the later introduction of additional structural elements.
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