7PL9

Cryo-EM structure of Bestrhodopsin (rhodopsin-rhodopsin-bestrophin) complex

7PL9 の概要

• エントリーDOI: 10.2210/pdb7pl9/pdb
• EMDBエントリー: 13485
• 分子名称: Rhodopsin, RETINAL (2 entities in total)
• 機能のキーワード: single particle cryo-em, membrane protein, rhodopsin
• 由来する生物種: Phaeocystis
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 671473.43

構造登録者

Matzov, D.,Kaczmarczyk, I.,Shalev-Benami, M. (登録日: 2021-08-29, 公開日: 2022-07-06)

主引用文献

Rozenberg, A.,Kaczmarczyk, I.,Matzov, D.,Vierock, J.,Nagata, T.,Sugiura, M.,Katayama, K.,Kawasaki, Y.,Konno, M.,Nagasaka, Y.,Aoyama, M.,Das, I.,Pahima, E.,Church, J.,Adam, S.,Borin, V.A.,Chazan, A.,Augustin, S.,Wietek, J.,Dine, J.,Peleg, Y.,Kawanabe, A.,Fujiwara, Y.,Yizhar, O.,Sheves, M.,Schapiro, I.,Furutani, Y.,Kandori, H.,Inoue, K.,Hegemann, P.,Beja, O.,Shalev-Benami, M.
Rhodopsin-bestrophin fusion proteins from unicellular algae form gigantic pentameric ion channels.
Nat.Struct.Mol.Biol., 29:592-603, 2022

PubMed Abstract: Many organisms sense light using rhodopsins, photoreceptive proteins containing a retinal chromophore. Here we report the discovery, structure and biophysical characterization of bestrhodopsins, a microbial rhodopsin subfamily from marine unicellular algae, in which one rhodopsin domain of eight transmembrane helices or, more often, two such domains in tandem, are C-terminally fused to a bestrophin channel. Cryo-EM analysis of a rhodopsin-rhodopsin-bestrophin fusion revealed that it forms a pentameric megacomplex (~700 kDa) with five rhodopsin pseudodimers surrounding the channel in the center. Bestrhodopsins are metastable and undergo photoconversion between red- and green-absorbing or green- and UVA-absorbing forms in the different variants. The retinal chromophore, in a unique binding pocket, photoisomerizes from all-trans to 11-cis form. Heterologously expressed bestrhodopsin behaves as a light-modulated anion channel.

PubMed: 35710843
DOI: 10.1038/s41594-022-00783-x

実験手法

ELECTRON MICROSCOPY (3.21 Å)