Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.

ABSTRACT: Channelrhodopsins, light-gated cation channels, enable precise control of neural cell depolarization or hyperpolarization with light in the field of optogenetics. This study integrates time-resolved serial crystallography and atomistic molecular dynamics (MD) simulations to resolve the structural changes during C1C2 channelrhodopsin activation. Our observations reveal that within the crystal environment, C1C2 predominantly remains in a light-activated state with characteristics of the M₃₉₀ intermediate. Here, rearrangement of retinal within its binding pocket partially opens the central gate toward the extracellular vestibule. These structural changes initiate channel opening but were insufficient to allow K⁺ flow. Adjusting protonation states to represent the subsequ

SUBMITTER: Mulder M 

PROVIDER: S-EPMC11726564 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature