3UG9

Crystal Structure of the Closed State of Channelrhodopsin

3UG9 の概要

• エントリーDOI: 10.2210/pdb3ug9/pdb
• 関連するPDBエントリー: 3UGA
• 分子名称: Archaeal-type opsin 1, Archaeal-type opsin 2, RETINAL, OLEIC ACID, ... (4 entities in total)
• 機能のキーワード: microbialrhodopsin, seven-transmembrane, light-gated cation channel, membrane protein
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 39421.19

構造登録者

Kato, H.E.,Ishitani, R.,Nureki, O. (登録日: 2011-11-02, 公開日: 2012-01-25, 最終更新日: 2024-11-20)

主引用文献

Kato, H.E.,Zhang, F.,Yizhar, O.,Ramakrishnan, C.,Nishizawa, T.,Hirata, K.,Ito, J.,Aita, Y.,Tsukazaki, T.,Hayashi, S.,Hegemann, P.,Maturana, A.D.,Ishitani, R.,Deisseroth, K.,Nureki, O.
Crystal structure of the channelrhodopsin light-gated cation channel
Nature, 482:369-374, 2012

PubMed Abstract: Channelrhodopsins (ChRs) are light-gated cation channels derived from algae that have shown experimental utility in optogenetics; for example, neurons expressing ChRs can be optically controlled with high temporal precision within systems as complex as freely moving mammals. Although ChRs have been broadly applied to neuroscience research, little is known about the molecular mechanisms by which these unusual and powerful proteins operate. Here we present the crystal structure of a ChR (a C1C2 chimaera between ChR1 and ChR2 from Chlamydomonas reinhardtii) at 2.3 Å resolution. The structure reveals the essential molecular architecture of ChRs, including the retinal-binding pocket and cation conduction pathway. This integration of structural and electrophysiological analyses provides insight into the molecular basis for the remarkable function of ChRs, and paves the way for the precise and principled design of ChR variants with novel properties.

PubMed: 22266941
DOI: 10.1038/nature10870

実験手法

X-RAY DIFFRACTION (2.3 Å)