7ZBE

Dark state crystal structure of bovine rhodopsin in Lipidic Cubic Phase (SwissFEL)

7ZBE の概要

• エントリーDOI: 10.2210/pdb7zbe/pdb
• 分子名称: Rhodopsin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ACETYL GROUP, ... (9 entities in total)
• 機能のキーワード: gpcr, opsin, xfel, membrane protein
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85359.30

構造登録者

Gruhl, T.,Weinert, T.,Rodrigues, M.J.,Milne, C.,Ortolani, G.,Nass, K.,Nango, E.,Sen, S.,Johnson, P.,Cirelli, C.,Furrer, A.,Mous, S.,Skopintsev, P.,James, D.,Dworkowski, F.,Baath, P.,Kekilli, D.,Oserov, D.,Tanaka, R.,Glover, H.,Bacellar, C.,Bruenle, S.,Casadei, C.,Diethelm, A.,Gashi, D.,Gotthard, G.,Guixa-Gonzalez, R.,Joti, Y.,Kabanova, V.,Knopp, G.,Lesca, E.,Ma, P.,Martiel, I.,Muehle, J.,Owada, S.,Pamula, F.,Sarabi, D.,Tejero, O.,Tsai, C.J.,Varma, N.,Wach, A.,Boutet, S.,Tono, K.,Nogly, P.,Deupi, X.,Iwata, S.,Neutze, R.,Standfuss, J.,Schertler, G.F.X.,Panneels, V. (登録日: 2022-03-23, 公開日: 2023-03-29, 最終更新日: 2024-02-07)

主引用文献

Gruhl, T.,Weinert, T.,Rodrigues, M.J.,Milne, C.J.,Ortolani, G.,Nass, K.,Nango, E.,Sen, S.,Johnson, P.J.M.,Cirelli, C.,Furrer, A.,Mous, S.,Skopintsev, P.,James, D.,Dworkowski, F.,Bath, P.,Kekilli, D.,Ozerov, D.,Tanaka, R.,Glover, H.,Bacellar, C.,Brunle, S.,Casadei, C.M.,Diethelm, A.D.,Gashi, D.,Gotthard, G.,Guixa-Gonzalez, R.,Joti, Y.,Kabanova, V.,Knopp, G.,Lesca, E.,Ma, P.,Martiel, I.,Muhle, J.,Owada, S.,Pamula, F.,Sarabi, D.,Tejero, O.,Tsai, C.J.,Varma, N.,Wach, A.,Boutet, S.,Tono, K.,Nogly, P.,Deupi, X.,Iwata, S.,Neutze, R.,Standfuss, J.,Schertler, G.,Panneels, V.
Ultrafast structural changes direct the first molecular events of vision.
Nature, 615:939-944, 2023

PubMed Abstract: Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs). A photon is absorbed by the 11-cis retinal chromophore of rhodopsin, which isomerizes within 200 femtoseconds to the all-trans conformation, thereby initiating the cellular signal transduction processes that ultimately lead to vision. However, the intramolecular mechanism by which the photoactivated retinal induces the activation events inside rhodopsin remains experimentally unclear. Here we use ultrafast time-resolved crystallography at room temperature to determine how an isomerized twisted all-trans retinal stores the photon energy that is required to initiate the protein conformational changes associated with the formation of the G protein-binding signalling state. The distorted retinal at a 1-ps time delay after photoactivation has pulled away from half of its numerous interactions with its binding pocket, and the excess of the photon energy is released through an anisotropic protein breathing motion in the direction of the extracellular space. Notably, the very early structural motions in the protein side chains of rhodopsin appear in regions that are involved in later stages of the conserved class A GPCR activation mechanism. Our study sheds light on the earliest stages of vision in vertebrates and points to fundamental aspects of the molecular mechanisms of agonist-mediated GPCR activation.

PubMed: 36949205
DOI: 10.1038/s41586-023-05863-6

実験手法

X-RAY DIFFRACTION (1.8 Å)