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Publication Abstract from PubMed

Rhodopsin (Rho), a prototypical G-protein-coupled receptor (GPCR) in vertebrate vision, activates the G-protein transducin (GT) by catalyzing GDP-GTP exchange on its alpha subunit (GalphaT). To elucidate the determinants of GT coupling and activation, we obtained cryo-EM structures of a fully functional, light-activated Rho-GT complex in the presence and absence of a G-protein-stabilizing nanobody. The structures illustrate how GT overcomes its low basal activity by engaging activated Rho in a conformation distinct from other GPCR-G-protein complexes. Moreover, the nanobody-free structures reveal native conformations of G-protein components and capture three distinct conformers showing the GalphaT helical domain (alphaHD) contacting the Gbetagamma subunits. These findings uncover the molecular underpinnings of G-protein activation by visual rhodopsin and shed new light on the role played by Gbetagamma during receptor-catalyzed nucleotide exchange.

Structures of the Rhodopsin-Transducin Complex: Insights into G-Protein Activation.,Gao Y, Hu H, Ramachandran S, Erickson JW, Cerione RA, Skiniotis G Mol Cell. 2019 Jun 24. pii: S1097-2765(19)30440-X. doi:, 10.1016/j.molcel.2019.06.007. PMID:31300275^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.