Asymmetric Nature of MscL Opening Revealed by Molecular Dynamics Simulations.

ABSTRACT: The bacterial mechanosensitive channel, MscL, opens in response to elevated membrane tension during osmotic shock. Some mutations, like L17A and V21A, can reduce the activation tension threshold, thus offering an approach to study the mechanism of MscL gating. We employed all-atom molecular dynamics to simulate the L17A, V21A double mutant of MscL under a tension of 30 mN/m. Under these conditions, the closed state initially adopts a funnel-like conformation. Subsequently, five chains of MscL undergo sequential transitions into asymmetric states (S1, S2, etc.). Within its "open" fragment, the S1 state is similar to the expanded state of Methanosarcina acetivorans MscL and has a conductance 10 times lower than the open state. We applied committor analysis and a nonlinear regression m

SUBMITTER: Rogacheva ON 

PROVIDER: S-EPMC12199302 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature