6EDQ

Crystal Structure of the Light-Gated Anion Channelrhodopsin GtACR1

6EDQ の概要

• エントリーDOI: 10.2210/pdb6edq/pdb
• 分子名称: Anion channelrhodopsin 1, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: cl- channel, membrane proteins, membrane protein
• 由来する生物種: Guillardia theta CCMP2712
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 72651.90

構造登録者

Li, H.,Huang, C.Y.,Wang, M.,Zheng, L.,Spudich, J.L. (登録日: 2018-08-10, 公開日: 2019-01-16, 最終更新日: 2023-10-11)

主引用文献

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

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: 30614787
DOI: 10.7554/eLife.41741

実験手法

X-RAY DIFFRACTION (2.9 Å)