8A6E

100 picosecond light activated crystal structure of bovine rhodopsin in Lipidic Cubic Phase (SACLA)

Summary for 8A6E

• Entry DOI: 10.2210/pdb8a6e/pdb
• Descriptor: Rhodopsin, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, RETINAL, ... (8 entities in total)
• Functional Keywords: gpcr, opsin, membrane protein
• Biological source: Bos taurus (cattle)
• Total number of polymer chains: 2
• Total formula weight: 85323.26

Authors

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.,Baath, P.,Kekilli, D.,Oserov, D.,Tanaka, R.,Glover, H.,Bacellar, C.,Bruenle, 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.,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. (deposition date: 2022-06-17, release date: 2023-03-29, Last modification date: 2024-11-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)