9go2

C1C2 Channelrhodopsin - SMX Light activated structure

spinqualitylabelsall models 9go2, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9go2 is a 1 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: OLC, RET Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8RUT8_CHLRE Q93WP2_CHLRE Publication Abstract from PubMed 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 M(390) 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 subsequent N(520) intermediate in our MD simulations induced further conformational changes, including rearrangements of transmembrane helices 2 and 7, that opened the inner gate and the putative ion-translocation pathway. This allowed spontaneous cation conduction with low conductance, aligning with experimental findings. Our findings provide critical structural insights into key intermediates of the channel opening mechanism, enhancing our understanding of ion conduction and selectivity in channelrhodopsins at an atomistic level. Structural Insights Into the Opening Mechanism of C1C2 Channelrhodopsin.,Mulder M, Hwang S, Broser M, Brunle S, Skopintsev P, Schattenberg C, Schnick C, Hartmann S, Church J, Schapiro I, Dworkowski F, Weinert T, Hegemann P, Sun H, Standfuss J J Am Chem Soc. 2025 Jan 8;147(1):1282-1290. doi: 10.1021/jacs.4c15402. Epub 2024 , Dec 16. PMID:39680650 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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