6edq

Crystal Structure of the Light-Gated Anion Channelrhodopsin GtACR1

spinqualitylabelsall models 6edq, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6edq is a 2 chain structure with sequence from Guillardia theta CCMP2712. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: GOL, LYR, OLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L1J207_GUITC Publication Abstract from PubMed The anion channelrhodopsin GtACR1 from the alga Guillardia theta is a potent neuron-inhibiting optogenetics tool. Presented here, its X-ray structure at 2.9 A reveals a tunnel traversing the protein from its extracellular surface to a large cytoplasmic cavity. The tunnel is lined primarily by small polar and aliphatic residues essential for anion conductance. A disulfide-immobilized extracellular cap facilitates channel closing and the ion path is blocked mid-membrane by its photoactive retinylidene chromophore and further by a cytoplasmic side constriction. The structure also reveals a novel photoactive site configuration that maintains the retinylidene Schiff base protonated when the channel is open. These findings suggest a new channelrhodopsin mechanism, in which the Schiff base not only controls gating, but also serves as a direct mediator for anion flux. Crystal structure of a natural light-gated anion channelrhodopsin.,Li H, Huang CY, Govorunova EG, Schafer CT, Sineshchekov OA, Wang M, Zheng L, Spudich JL Elife. 2019 Jan 7;8. pii: 41741. doi: 10.7554/eLife.41741. PMID:30614787 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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