ArticleBiophysical journal2014
Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance.
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 23 papers.
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Who cites it
23 citing papers in PubMed.
- Protocol for preparing and characterizing samples for combined microsecond freeze-hyperquenching and electron paramagnetic resonance spectroscopy.STAR protocols · 2026Article
- Genetic and cellular characterization of MscS-like putative channels in the filamentous fungusChannels (Austin, Tex.) · 2022Article
- HDX-guided EPR spectroscopy to interrogate membrane protein dynamics.STAR protocols · 2022Article
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- PELDOR Measurements on Nitroxide-Labeled Oligonucleotides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Spin Labeling of Long RNAs Via Click Reaction and Enzymatic Ligation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.Biophysical journal · 2020Article
- PELDOR/DEER: An Electron Paramagnetic Resonance Method to Study Membrane Proteins in Lipid Bilayers.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets.Nature communications · 2019Article
- Coiled-coil formation of the membrane-fusion K/E peptides viewed by electron paramagnetic resonance.PloS one · 2018Article
- Sparse Labeling PELDOR Spectroscopy on Multimeric Mechanosensitive Membrane Channels.Biophysical journal · 2017Article
- Structural basis for antibacterial peptide self-immunity by the bacterial ABC transporter McjD.The EMBO journal · 2017Article
- Enhanced imaging of lipid rich nanoparticles embedded in methylcellulose films for transmission electron microscopy using mixtures of heavy metals.Micron (Oxford, England : 1993) · 2017Article
- Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21.Biophysical journal · 2016Article
- Nanoparticle suspensions enclosed in methylcellulose: a new approach for quantifying nanoparticles in transmission electron microscopy.Scientific reports · 2016Article
- Accurate Extraction of Nanometer Distances in Multimers by Pulse EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2016Article
- Taking a molecular motor for a spin: helicase mechanism studied by spin labeling and PELDOR.Nucleic acids research · 2016Article
- The role of lipids in mechanosensation.Nature structural & molecular biology · 2015Article
- The Structure of YnaI Implies Structural and Mechanistic Conservation in the MscS Family of Mechanosensitive Channels.Structure (London, England : 1993) · 2015Article
- Properties of the Mechanosensitive Channel MscS Pore Revealed by Tryptophan Scanning Mutagenesis.Biochemistry · 2015Article
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Authors and funding
11 authors.
Funding
Abstract
Mechanosensitive channel proteins are important safety valves against osmotic shock in bacteria, and are involved in sensing touch and sound waves in higher organisms. The mechanosensitive channel of small conductance (MscS) has been extensively studied. Pulsed electron-electron double resonance (PELDOR or DEER) of detergent-solubilized protein confirms that as seen in the crystal structure, the outer ring of transmembrane helices do not pack against the pore-forming helices, creating an apparent void. The relevance of this void to the functional form of MscS in the bilayer is the subject of debate. Here, we report PELDOR measurements of MscS reconstituted into two lipid bilayer systems: nanodiscs and bicelles. The distance measurements from multiple mutants derived from the PELDOR data are consistent with the detergent-solution arrangement of the protein. We conclude, therefore, that the relative positioning of the transmembrane helices is preserved in mimics of the cell bilayer, and that the apparent voids are not an artifact of detergent solution but a property of the protein that will have to be accounted for in any molecular mechanism of gating.
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