ArticleProtein science : a publication of the Protein Society2008
The structure of the lipid-embedded potassium channel voltage sensor determined by double-electron-electron resonance spectroscopy.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed.
- Structural Dynamics of the Slide Helix of Inactive/Closed Conformation of KirBac1.1 in Micelles and Membranes: A Fluorescence Approach.The Journal of membrane biology · 2025Article
- Characterization of a novel MgtE homolog and its structural dynamics in membrane mimetics.Biophysical journal · 2024Article
- Revealing the DNA Binding Modes of CsoR by EPR Spectroscopy.ACS omega · 2023Article
- An EPR Study on the Interaction between the Cu(I) Metal Binding Domains of ATP7B and the Atox1 Metallochaperone.International journal of molecular sciences · 2020Article
- Cu(I) Controls Conformational States in Human Atox1 Metallochaperone: An EPR and Multiscale Simulation Study.The journal of physical chemistry. B · 2020Article
- Structural Dynamics of the Paddle Motif Loop in the Activated Conformation of KvAP Voltage Sensor.Biophysical journal · 2020Article
- Unraveling the Impact of Cysteine-to-Serine Mutations on the Structural and Functional Properties of Cu(I)-Binding Proteins.International journal of molecular sciences · 2019Article
- The structural flexibility of the human copper chaperone Atox1: Insights from combined pulsed EPR studies and computations.Protein science : a publication of the Protein Society · 2017Article
- EPR Studies of Gating Mechanisms in Ion Channels.Methods in enzymology · 2015Review
- Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance.Biophysical journal · 2014Article
- Voltage sensor ring in a native structure of a membrane-embedded potassium channel.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Conformational ensemble of the sodium-coupled aspartate transporter.Nature structural & molecular biology · 2013Article
- Position and motions of the S4 helix during opening of the Shaker potassium channel.The Journal of general physiology · 2010Article
- Electron spin-echo envelope modulation (ESEEM) reveals water and phosphate interactions with the KcsA potassium channel.Biochemistry · 2010Article
- Article
- Combining electron crystallography and X-ray crystallography to study the MlotiK1 cyclic nucleotide-regulated potassium channel.Journal of structural biology · 2009Article
- Pulsed EPR determination of water accessibility to spin-labeled amino acid residues in LHCIIb.Biophysical journal · 2009Article
- Sensing voltage across lipid membranes.Nature · 2008Review
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5 authors.
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Abstract
A four-pulse electron paramagnetic resonance experiment was used to measure long-range inter-subunit distances in reconstituted KvAP, a voltage-dependent potassium (Kv) channel. The measurements have allowed us to reach the following five conclusions about the native structure of the voltage sensor of KvAP. First, the S1 helix of the voltage sensor engages in a helix packing interaction with the pore domain. Second, the crystallographically observed antiparallel helix-turn-helix motif of the voltage-sensing paddle is retained in the membrane-embedded voltage sensor. Third, the paddle is oriented in such a way as to expose one face to the pore domain and the opposite face to the membrane. Fourth, the paddle and the pore domain appear to be separated by a gap that is sufficiently wide for lipids to penetrate between the two domains. Fifth, the critical voltage-sensing arginine residues on the paddle appear to be lipid exposed. These results demonstrate the importance of the membrane for the native structure of Kv channels, suggest that lipids are an integral part of their native structure, and place the voltage-sensing machinery into a complex lipid environment near the pore domain.
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