ArticleProceedings of the National Academy of Sciences of the United States of America2015
Mechanical coupling of the multiple structural elements of the large-conductance mechanosensitive channel during expansion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 51 citations in OpenAlex.
- 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.Research square · 2026Article
- Overexpression of the Large-Conductance Mechanosensitive Channel Gene inMicroorganisms · 2026Article
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Mechanism of capsaicin entry into buried vanilloid sites in TRPV1.Nature chemical biology · 2025Article
- Article
- Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.Journal of chemical information and modeling · 2025Article
- Mechanosensitive channel MscL gating transitions coupling with constriction point shift.Protein science : a publication of the Protein Society · 2024Article
- Membrane Protein Structures in Native Cellular Membranes Revealed by Solid-State NMR Spectroscopy.JACS Au · 2023Article
- Solid-state NMR structure determination of a membrane protein inScience advances · 2023Article
- Approaches for the modulation of mechanosensitive MscL channel pores.Frontiers in chemistry · 2023Review
- Activation of a Bacterial Mechanosensitive Channel, MscL, Underlies the Membrane Permeabilization of Dual-Targeting Antibacterial Compounds.Antibiotics (Basel, Switzerland) · 2022Article
- Pocket delipidation induced by membrane tension or modification leads to a structurally analogous mechanosensitive channel state.Structure (London, England : 1993) · 2022Article
- In Silico Screen Identifies a New Family of Agonists for the Bacterial Mechanosensitive Channel MscL.Antibiotics (Basel, Switzerland) · 2022Article
- Mechanosensitive Channels Mediate Hypoionic Shock-Induced Aminoglycoside Potentiation against Bacterial Persisters by Enhancing Antibiotic Uptake.Antimicrobial agents and chemotherapy · 2022Article
- Nanchung and Inactive define pore properties of the native auditory transduction channel inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Model of Environmental Membrane Field for Transmembrane Proteins.International journal of molecular sciences · 2021Article
- Review
- In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.Biophysical journal · 2020Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The prokaryotic mechanosensitive channel of large conductance (MscL) is a pressure-relief valve protecting the cell from lysing during acute osmotic downshock. When the membrane is stretched, MscL responds to the increase of membrane tension and opens a nonselective pore to about 30 Å wide, exhibiting a large unitary conductance of ∼ 3 nS. A fundamental step toward understanding the gating mechanism of MscL is to decipher the molecular details of the conformational changes accompanying channel opening. By applying fusion-protein strategy and controlling detergent composition, we have solved the structures of an archaeal MscL homolog from Methanosarcina acetivorans trapped in the closed and expanded intermediate states. The comparative analysis of these two new structures reveals significant conformational rearrangements in the different domains of MscL. The large changes observed in the tilt angles of the two transmembrane helices (TM1 and TM2) fit well with the helix-pivoting model derived from the earlier geometric analyses based on the previous structures. Meanwhile, the periplasmic loop region transforms from a folded structure, containing an ω-shaped loop and a short β-hairpin, to an extended and partly disordered conformation during channel expansion. Moreover, a significant rotating and sliding of the N-terminal helix (N-helix) is coupled to the tilting movements of TM1 and TM2. The dynamic relationships between the N-helix and TM1/TM2 suggest that the N-helix serves as a membrane-anchored stopper that limits the tilts of TM1 and TM2 in the gating process. These results provide direct mechanistic insights into the highly coordinated movement of the different domains of the MscL channel when it expands.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.