8R0O

Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 10.5 in detergent in the M state

8R0O の概要

• エントリーDOI: 10.2210/pdb8r0o/pdb
• EMDBエントリー: 18799
• 分子名称: Rhodopsin, DODECYL-BETA-D-MALTOSIDE, RETINAL, ... (4 entities in total)
• 機能のキーワード: rhodopsin, retinal, cryo-em, light sensor, membrane protein
• 由来する生物種: Cryobacterium levicorallinum; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 180010.08

構造登録者

Kovalev, K.,Marin, E.,Stetsenko, A.,Guskov, A.,Lamm, G.H.U. (登録日: 2023-10-31, 公開日: 2025-05-14, 最終更新日: 2025-07-16)

主引用文献

Lamm, G.H.U.,Marin, E.,Alekseev, A.,Schellbach, A.V.,Stetsenko, A.,Haro-Moreno, J.M.,Bourenkov, G.,Borshchevskiy, V.,Asido, M.,Agthe, M.,Engilberge, S.,Rose, S.L.,Caramello, N.,Royant, A.,Schneider, T.R.,Bateman, A.,Mager, T.,Moser, T.,Rodriguez-Valera, F.,Wachtveitl, J.,Guskov, A.,Kovalev, K.
CryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.
Sci Adv, 11:eadv1015-eadv1015, 2025

PubMed Abstract: Microbial rhodopsins are omnipresent on Earth; however, the vast majority of them remain uncharacterized. Here, we describe a rhodopsin group found in microorganisms from cold environments, such as glaciers, denoted as CryoRhodopsins (CryoRs). A distinguishing feature of the group is the presence of a buried arginine residue close to the cytoplasmic face. Combining single-particle cryo-electron microscopy and x-ray crystallography with rhodopsin activation by light, we demonstrate that the arginine stabilizes an ultraviolet (UV)-absorbing intermediate of an extremely slow CryoRhodopsin photocycle. Together with extensive spectroscopic characterization, our investigations on CryoR1 and CryoR2 proteins reveal mechanisms of photoswitching in the identified group. Our data suggest that CryoRs are sensors for UV irradiation and are also capable of inward proton translocation modulated by UV light.

PubMed: 40614199
DOI: 10.1126/sciadv.adv1015

実験手法

ELECTRON MICROSCOPY (2.3 Å)