Journal
ELIFE
Volume 8, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.41741
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Funding
- National Institutes of Health [R01GM027750, U01MH109146]
- Welch Foundation [AU-0009]
- American Heart Association [18TPA34230046]
- Hermann Eye Fund
- H2020 Marie Sklodowska-Curie Actions [701647]
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The anion channelrhodopsin GtACR1 from the alga Guillardia theta is a potent neuroninhibiting optogenetics tool. Presented here, its X-ray structure at 2.9 angstrom 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.
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