6QNO

Rhodopsin-Gi protein complex

6QNO の概要

• エントリーDOI: 10.2210/pdb6qno/pdb
• EMDBエントリー: 4598
• 分子名称: Guanine nucleotide-binding protein G(i) subunit alpha-1, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(T) subunit gamma-T1, ... (8 entities in total)
• 機能のキーワード: gpcr and g protein complex, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 181773.74

構造登録者

Tsai, C.-J.,Marino, J.,Adaixo, R.J.,Pamula, F.,Muehle, J.,Maeda, S.,Flock, T.,Taylor, N.M.I.,Mohammed, I.,Matile, H.,Dawson, R.J.P.,Deupi, X.,Stahlberg, H.,Schertler, G.F.X. (登録日: 2019-02-11, 公開日: 2019-07-10, 最終更新日: 2024-11-06)

主引用文献

Tsai, C.J.,Marino, J.,Adaixo, R.,Pamula, F.,Muehle, J.,Maeda, S.,Flock, T.,Taylor, N.M.,Mohammed, I.,Matile, H.,Dawson, R.J.,Deupi, X.,Stahlberg, H.,Schertler, G.
Cryo-EM structure of the rhodopsin-G alpha i-beta gamma complex reveals binding of the rhodopsin C-terminal tail to the G beta subunit.
Elife, 8:-, 2019

PubMed Abstract: One of the largest membrane protein families in eukaryotes are G protein-coupled receptors (GPCRs). GPCRs modulate cell physiology by activating diverse intracellular transducers, prominently heterotrimeric G proteins. The recent surge in structural data has expanded our understanding of GPCR-mediated signal transduction. However, many aspects, including the existence of transient interactions, remain elusive. We present the cryo-EM structure of the light-sensitive GPCR rhodopsin in complex with heterotrimeric Gi. Our density map reveals the receptor C-terminal tail bound to the Gβ subunit of the G protein, providing a structural foundation for the role of the C-terminal tail in GPCR signaling, and of Gβ as scaffold for recruiting Gα subunits and G protein-receptor kinases. By comparing available complexes, we found a small set of common anchoring points that are G protein-subtype specific. Taken together, our structure and analysis provide new structural basis for the molecular events of the GPCR signaling pathway.

PubMed: 31251171
DOI: 10.7554/eLife.46041

実験手法

ELECTRON MICROSCOPY (4.38 Å)