6FUF

Crystal structure of the rhodopsin-mini-Go complex

Summary for 6FUF

• Entry DOI: 10.2210/pdb6fuf/pdb
• Descriptor: Rhodopsin, Guanine nucleotide-binding protein G(o) subunit alpha, RETINAL, ... (5 entities in total)
• Functional Keywords: gpcr complex rhodopsin, signaling protein
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 2
• Total formula weight: 60624.39

Authors

Tsai, C.-J.,Weinert, T.,Muehle, J.,Pamula, F.,Nehme, R.,Flock, T.,Nogly, P.,Edwards, P.C.,Carpenter, B.,Gruhl, T.,Ma, P.,Deupi, X.,Standfuss, J.,Tate, C.G.,Schertler, G.F.X. (deposition date: 2018-02-27, release date: 2018-10-03, Last modification date: 2024-11-13)

Primary citation

Tsai, C.J.,Pamula, F.,Nehme, R.,Muhle, J.,Weinert, T.,Flock, T.,Nogly, P.,Edwards, P.C.,Carpenter, B.,Gruhl, T.,Ma, P.,Deupi, X.,Standfuss, J.,Tate, C.G.,Schertler, G.F.X.
Crystal structure of rhodopsin in complex with a mini-Gosheds light on the principles of G protein selectivity.
Sci Adv, 4:eaat7052-eaat7052, 2018

PubMed Abstract: Selective coupling of G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors (GPCRs) to specific Gα-protein subtypes is critical to transform extracellular signals, carried by natural ligands and clinical drugs, into cellular responses. At the center of this transduction event lies the formation of a signaling complex between the receptor and G protein. We report the crystal structure of light-sensitive GPCR rhodopsin bound to an engineered mini-G protein. The conformation of the receptor is identical to all previous structures of active rhodopsin, including the complex with arrestin. Thus, rhodopsin seems to adopt predominantly one thermodynamically stable active conformation, effectively acting like a "structural switch," allowing for maximum efficiency in the visual system. Furthermore, our analysis of the well-defined GPCR-G protein interface suggests that the precise position of the carboxyl-terminal "hook-like" element of the G protein (its four last residues) relative to the TM7/helix 8 (H8) joint of the receptor is a significant determinant in selective G protein activation.

PubMed: 30255144
DOI: 10.1126/sciadv.aat7052

Experimental method

X-RAY DIFFRACTION (3.117 Å)