ArticleScientific reports2017
Structural Dynamics of the MscL C-terminal Domain.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Atomic structure and dynamics of the mechanosensitive channel MscL fromScience advances · 2026Article
- Structural basis of the gating mechanism of the large-conductance mechanosensitive channel from Escherichia coli.Nature communications · 2026Article
- Opening threshold and kinetics of the MscL mechanosensitive channel are regulated by its periplasmic loop.npj biological physics and mechanics · 2026Article
- Probing the mechanical properties of ORF3a protein, a transmembrane channel of SARS-CoV-2 virus: Molecular dynamics study.Chemical physics · 2023Article
- How Functional Lipids Affect the Structure and Gating of Mechanosensitive MscS-like Channels.International journal of molecular sciences · 2022Review
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- Elucidating the molecular basis of spontaneous activation in an engineered mechanosensitive channel.Computational and structural biotechnology journal · 2022Article
- Photoactivation of a Mechanosensitive Channel.Frontiers in molecular biosciences · 2022Article
- Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- Advances in high-speed atomic force microscopy (HS-AFM) reveal dynamics of transmembrane channels and transporters.Current opinion in structural biology · 2019Review
- Conformational Changes and Membrane Interaction of the Bacterial Phospholipase, ExoU: Characterization by Site-Directed Spin Labeling.Cell biochemistry and biophysics · 2019Article
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Authors and funding
9 authors.
Funding
Abstract
The large conductance mechanosensitive channel (MscL), acts as an osmoprotective emergency valve in bacteria by opening a large, water-filled pore in response to changes in membrane tension. In its closed configuration, the last 36 residues at the C-terminus form a bundle of five α-helices co-linear with the five-fold axis of symmetry. Here, we examined the structural dynamics of the C-terminus of EcMscL using site-directed spin labelling electron paramagnetic resonance (SDSL EPR) spectroscopy. These experiments were complemented with computational modelling including molecular dynamics (MD) simulations and finite element (FE) modelling. Our results show that under physiological conditions, the C-terminus is indeed an α-helical bundle, located near the five-fold symmetry axis of the molecule. Both experiments and computational modelling demonstrate that only the top part of the C-terminal domain (from the residue A110 to E118) dissociates during the channel gating, while the rest of the C-terminus stays assembled. This result is consistent with the view that the C-terminus functions as a molecular sieve and stabilizer of the oligomeric MscL structure as previously suggested.
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