9EPQ

Cryo-EM Structure of Jumping Spider Rhodopsin-1 bound to a Giq heterotrimer

This is a non-PDB format compatible entry.

Summary for 9EPQ

• Entry DOI: 10.2210/pdb9epq/pdb
• EMDB information: 19883
• Descriptor: Kumopsin1, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (5 entities in total)
• Functional Keywords: opsin, gpcr, g protein, signaling complex, membrane protein
• Biological source: Hasarius adansoni; More
• Total number of polymer chains: 4
• Total formula weight: 121837.21

Authors

Tejero, O.,Pamula, F.,Koyanagi, M.,Nagata, T.,Afanasyev, P.,Das, I.,Deupi, X.,Sheves, M.,Terakita, A.,Schertler, G.F.X.,Rodrigues, M.J.,Tsai, C.-J. (deposition date: 2024-03-19, release date: 2024-10-23, Last modification date: 2024-11-06)

Primary citation

Tejero, O.,Pamula, F.,Koyanagi, M.,Nagata, T.,Afanasyev, P.,Das, I.,Deupi, X.,Sheves, M.,Terakita, A.,Schertler, G.F.X.,Rodrigues, M.J.,Tsai, C.J.
Active state structures of a bistable visual opsin bound to G proteins.
Nat Commun, 15:8928-8928, 2024

PubMed Abstract: Opsins are G protein-coupled receptors (GPCRs) that have evolved to detect light stimuli and initiate intracellular signaling cascades. Their role as signal transducers is critical to light perception across the animal kingdom. Opsins covalently bind to the chromophore 11-cis retinal, which isomerizes to the all-trans isomer upon photon absorption, causing conformational changes that result in receptor activation. Monostable opsins, responsible for vision in vertebrates, release the chromophore after activation and must bind another retinal molecule to remain functional. In contrast, bistable opsins, responsible for non-visual light perception in vertebrates and for vision in invertebrates, absorb a second photon in the active state to return the chromophore and protein to the inactive state. Structures of bistable opsins in the activated state have proven elusive, limiting our understanding of how they function as bidirectional photoswitches. Here we present active state structures of a bistable opsin, jumping spider rhodopsin isoform-1 (JSR1), in complex with its downstream signaling partners, the G and G heterotrimers. These structures elucidate key differences in the activation mechanisms between monostable and bistable opsins, offering essential insights for the rational engineering of bistable opsins into diverse optogenetic tools to control G protein signaling pathways.

PubMed: 39414813
DOI: 10.1038/s41467-024-53208-2

Experimental method

ELECTRON MICROSCOPY (4.15 Å)