Cryo-EM structure of human rhodopsin bound to an inhibitory G protein

Yanyong Kang, Oleg Kuybeda, Parker W. de Waal, Somnath Mukherjee, Ned Van Eps, Przemyslaw Dutka, X. Edward Zhou, Alberto Bartesaghi, Satchal Erramilli, Takefumi Morizumi, Xin Gu, Yanting Yin, Ping Liu, Yi Jiang, Xing Meng, Gongpu Zhao, Karsten Melcher, Oliver P. Ernst, Anthony A. Kossiakoff (), Sriram Subramaniam () and H. Eric Xu ()
Additional contact information
Yanyong Kang: Van Andel Research Institute
Oleg Kuybeda: Frederick National Laboratory for Cancer Research
Parker W. de Waal: Van Andel Research Institute
Somnath Mukherjee: University of Chicago
Ned Van Eps: University of Toronto
Przemyslaw Dutka: University of Chicago
X. Edward Zhou: Van Andel Research Institute
Alberto Bartesaghi: Frederick National Laboratory for Cancer Research
Satchal Erramilli: University of Chicago
Takefumi Morizumi: University of Toronto
Xin Gu: Van Andel Research Institute
Yanting Yin: Van Andel Research Institute
Ping Liu: University of Chinese Academy of Sciences
Yi Jiang: Chinese Academy of Sciences
Xing Meng: Van Andel Research Institute
Gongpu Zhao: Van Andel Research Institute
Karsten Melcher: Van Andel Research Institute
Oliver P. Ernst: University of Toronto
Anthony A. Kossiakoff: University of Chicago
Sriram Subramaniam: Frederick National Laboratory for Cancer Research
H. Eric Xu: Van Andel Research Institute

Nature, 2018, vol. 558, issue 7711, 553-558

Abstract: 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 Gs (stimulatory) and Gi (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 Gi are mediated by the C-terminal helix of the Gi 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, Gi-bound and arrestin-bound forms of rhodopsin with inactive and Gs-bound forms of the β2-adrenergic receptor provide a foundation to understand the unique structural signatures that are associated with the recognition of Gs, Gi and arrestin by activated G-protein-coupled receptors.

Date: 2018
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DOI: 10.1038/s41586-018-0215-y

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