Atomic structure and dynamics of the mechanosensitive channel MscL from Escherichia coli by cryo-EM and solid-state NMR.

Cryo-EM and NMR reveal conformational changes and dynamics in Escherichia coli MscL, highlighting early gating transitions with significant heterogeneity in mutants.

• Why it matters: Understanding the structural basis of mechanosensitive channel gating is crucial for insights into cellular responses to membrane tension, yet remains incomplete, limiting potential for targeted manipulation.
• What they did: The study combined cryo-EM structures of wild-type and G22S mutant MscL in lipid nanodiscs with solid-state NMR measurements in liposomes, capturing both static structures and dynamic behavior.
• The result: Findings demonstrate that the G22S mutant exhibits increased conformational flexibility and early gating transitions, providing a framework for designing channels with adjustable gating properties.