Ultrafast structural changes direct the first molecular events of vision.

ABSTRACT: Vision is initiated by the rhodopsin family of light-sensitive G protein-coupled receptors (GPCRs)¹. A photon is absorbed by the 11-cis retinal chromophore of rhodopsin, which isomerizes within 200 femtoseconds to the all-trans conformation², 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 temperature³ 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 sig

SUBMITTER: Gruhl T 

PROVIDER: S-EPMC10060157 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature