6EDQ
Crystal Structure of the Light-Gated Anion Channelrhodopsin GtACR1
Summary for 6EDQ
| Entry DOI | 10.2210/pdb6edq/pdb |
| Descriptor | Anion channelrhodopsin 1, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | cl- channel, membrane proteins, membrane protein |
| Biological source | Guillardia theta CCMP2712 |
| Total number of polymer chains | 2 |
| Total formula weight | 72651.90 |
| Authors | Li, H.,Huang, C.Y.,Wang, M.,Zheng, L.,Spudich, J.L. (deposition date: 2018-08-10, release date: 2019-01-16, Last modification date: 2023-10-11) |
| Primary citation | Li, H.,Huang, C.Y.,Govorunova, E.G.,Schafer, C.T.,Sineshchekov, O.A.,Wang, M.,Zheng, L.,Spudich, J.L. Crystal structure of a natural light-gated anion channelrhodopsin. Elife, 8:-, 2019 Cited by PubMed Abstract: The anion channelrhodopsin ACR1 from the alga is a potent neuron-inhibiting optogenetics tool. Presented here, its X-ray structure at 2.9 Å 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. PubMed: 30614787DOI: 10.7554/eLife.41741 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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