6CMO

Rhodopsin-Gi complex

Summary for 6CMO

• Entry DOI: 10.2210/pdb6cmo/pdb
• EMDB information: 7517
• Descriptor: chimera protein of Soluble cytochrome b562 and Rhodopsin, Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, ... (7 entities in total)
• Functional Keywords: rhodopsin; g protein; cryo-em; structure, signaling protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 6
• Total formula weight: 187781.72

Authors

Kang, Y.,Kuybeda, O.,de Waal, P.W.,Mukherjee, S.,Van Eps, N.,Dutka, P.,Zhou, X.E.,Bartesaghi, A.,Erramilli, S.,Morizumi, T.,Gu, X.,Yin, Y.,Liu, P.,Jiang, Y.,Meng, X.,Zhao, G.,Melcher, K.,Earnst, O.P.,Kossiakoff, A.A.,Subramaniam, S.,Xu, H.E. (deposition date: 2018-03-05, release date: 2018-06-20, Last modification date: 2024-10-23)

Primary citation

Kang, Y.,Kuybeda, O.,de Waal, P.W.,Mukherjee, S.,Van Eps, N.,Dutka, P.,Zhou, X.E.,Bartesaghi, A.,Erramilli, S.,Morizumi, T.,Gu, X.,Yin, Y.,Liu, P.,Jiang, Y.,Meng, X.,Zhao, G.,Melcher, K.,Ernst, O.P.,Kossiakoff, A.A.,Subramaniam, S.,Xu, H.E.
Cryo-EM structure of human rhodopsin bound to an inhibitory G protein.
Nature, 558:553-558, 2018

PubMed Abstract: G-protein-coupled receptors comprise the largest family of mammalian transmembrane receptors. They mediate numerous cellular pathways by coupling with downstream signalling transducers, including the hetrotrimeric G proteins G (stimulatory) and G (inhibitory) and several arrestin proteins. The structural mechanisms that define how G-protein-coupled receptors selectively couple to a specific type of G protein or arrestin remain unknown. Here, using cryo-electron microscopy, we show that the major interactions between activated rhodopsin and G are mediated by the C-terminal helix of the G α-subunit, which is wedged into the cytoplasmic cavity of the transmembrane helix bundle and directly contacts the amino terminus of helix 8 of rhodopsin. Structural comparisons of inactive, G-bound and arrestin-bound forms of rhodopsin with inactive and G-bound forms of the β-adrenergic receptor provide a foundation to understand the unique structural signatures that are associated with the recognition of G, G and arrestin by activated G-protein-coupled receptors.

PubMed: 29899450
DOI: 10.1038/s41586-018-0215-y

Experimental method

ELECTRON MICROSCOPY (4.5 Å)