6OYA

Structure of the Rhodopsin-Transducin-Nanobody Complex

6OYA の概要

• エントリーDOI: 10.2210/pdb6oya/pdb
• EMDBエントリー: 20222 20223
• 分子名称: Gt-alpha/Gi1-alpha chimera, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(T) subunit gamma-T1, ... (6 entities in total)
• 機能のキーワード: gpcr, g protein, complex, signaling protein-immune system complex, signaling protein/immune system
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 142313.03

構造登録者

Gao, Y.,Hu, H.,Ramachandran, S.,Erickson, J.W.,Cerione, R.A.,Skiniotis, G. (登録日: 2019-05-14, 公開日: 2019-07-24, 最終更新日: 2024-11-06)

主引用文献

Gao, Y.,Hu, H.,Ramachandran, S.,Erickson, J.W.,Cerione, R.A.,Skiniotis, G.
Structures of the Rhodopsin-Transducin Complex: Insights into G-Protein Activation.
Mol.Cell, 75:781-, 2019

PubMed Abstract: Rhodopsin (Rho), a prototypical G-protein-coupled receptor (GPCR) in vertebrate vision, activates the G-protein transducin (G) by catalyzing GDP-GTP exchange on its α subunit (Gα). To elucidate the determinants of G coupling and activation, we obtained cryo-EM structures of a fully functional, light-activated Rho-G complex in the presence and absence of a G-protein-stabilizing nanobody. The structures illustrate how G 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 Gα helical domain (αHD) contacting the Gβγ subunits. These findings uncover the molecular underpinnings of G-protein activation by visual rhodopsin and shed new light on the role played by Gβγ during receptor-catalyzed nucleotide exchange.

PubMed: 31300275
DOI: 10.1016/j.molcel.2019.06.007

実験手法

ELECTRON MICROSCOPY (3.3 Å)