4X1H

Opsin/G(alpha) peptide complex stabilized by nonyl-glucoside

4X1H の概要

• エントリーDOI: 10.2210/pdb4x1h/pdb
• 分子名称: Rhodopsin, C-terminal derived peptide of guanine nucleotide-binding protein G(t) subunit alpha-1, beta-D-mannopyranose-(1-2)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total)
• 機能のキーワード: rhodopsin, gpcr, membrane protein, signaling protein
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42554.63

構造登録者

Blankenship, E.,Lodowski, D.T. (登録日: 2014-11-24, 公開日: 2015-11-04, 最終更新日: 2024-11-13)

主引用文献

Blankenship, E.,Vahedi-Faridi, A.,Lodowski, D.T.
The High-Resolution Structure of Activated Opsin Reveals a Conserved Solvent Network in the Transmembrane Region Essential for Activation.
Structure, 23:2358-2364, 2015

PubMed Abstract: Rhodopsin, a light-activated G protein coupled receptor (GPCR), has been the subject of numerous biochemical and structural investigations, serving as a model receptor for GPCRs and their activation. We present the 2.3-Å resolution structure of native source rhodopsin stabilized in a conformation competent for G protein binding. An extensive water-mediated hydrogen bond network linking the chromophore binding site to the site of G protein binding is observed, providing connections to conserved motifs essential for GPCR activation. Comparison of this extensive solvent-mediated hydrogen-bonding network with the positions of ordered solvent in earlier crystallographic structures of rhodopsin photointermediates reveals both static structural and dynamic functional water-protein interactions present during the activation process. When considered along with observations that solvent occupies similar positions in the structures of other GPCRs, these analyses strongly support an integral role for this dynamic ordered water network in both rhodopsin and GPCR activation.

PubMed: 26526852
DOI: 10.1016/j.str.2015.09.015

実験手法

X-RAY DIFFRACTION (2.29 Å)