6PW5

Cryo-EM Structure of Thermo-Sensitive TRP Channel TRP1 from the Alga Chlamydomonas reinhardtii in Nanodiscs

6PW5 の概要

• エントリーDOI: 10.2210/pdb6pw5/pdb
• EMDBエントリー: 20498 20499
• 分子名称: TRP-like ion channel, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE, ... (4 entities in total)
• 機能のキーワード: ion channels, membrane protein, trp channels, transport protein
• 由来する生物種: Chlamydomonas reinhardtii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 408173.68

構造登録者

McGoldrick, L.L.,Singh, A.K.,Sobolevsky, A.I. (登録日: 2019-07-22, 公開日: 2019-09-25, 最終更新日: 2024-11-20)

主引用文献

McGoldrick, L.L.,Singh, A.K.,Demirkhanyan, L.,Lin, T.Y.,Casner, R.G.,Zakharian, E.,Sobolevsky, A.I.
Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii.
Nat Commun, 10:4180-4180, 2019

PubMed Abstract: Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by which algae can detect and respond to changes in their environments can rely on membrane receptors, including TRP ion channels. Here we present a 3.5-Å resolution cryo-EM structure of the transient receptor potential (TRP) channel crTRP1 from the alga Chlamydomonas reinhardtii that opens in response to increased temperature and is positively regulated by the membrane lipid PIP. The structure of crTRP1 significantly deviates from the structures of other TRP channels and has a unique 2-fold symmetrical rose-shape architecture with elbow domains and ankyrin repeat domains submerged and dipping into the membrane, respectively. Our study provides a structure of a TRP channel from a micro-organism and a structural framework for better understanding algae biology and TRP channel evolution.

PubMed: 31519888
DOI: 10.1038/s41467-019-12121-9

実験手法

ELECTRON MICROSCOPY (3.45 Å)