2HPY

Crystallographic model of lumirhodopsin

2HPY の概要

• エントリーDOI: 10.2210/pdb2hpy/pdb
• 関連するPDBエントリー: 1U19 2G87
• 分子名称: Rhodopsin, HEPTANE-1,2,3-TRIOL, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
• 機能のキーワード: g protein-coupled receptor, visual pigment, signaling protein
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P02699
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 85393.66

構造登録者

Nakamichi, H.,Okada, T. (登録日: 2006-07-18, 公開日: 2006-08-22, 最終更新日: 2024-10-30)

主引用文献

Nakamichi, H.,Okada, T.
Local peptide movement in the photoreaction intermediate of rhodopsin
Proc.Natl.Acad.Sci.Usa, 103:12729-12734, 2006

PubMed Abstract: Photoactivation of the visual rhodopsin, a prototypical G protein-coupled receptor (GPCR), involves efficient conversion of the intrinsic inverse-agonist 11-cis-retinal to the all-trans agonist. This event leads to the rearrangement of the heptahelical transmembrane bundle, which is thought to be shared by hundreds of GPCRs. To examine this activation mechanism, we determined the x-ray crystallographic model of the photoreaction intermediate of rhodopsin, lumirhodopsin, which represents the conformational state having the nearly complete all-trans agonist form of the retinal. A difference electron density map clearly indicated that the distorted all-trans-retinal in the precedent intermediate bathorhodopsin relaxes by dislocation of the beta-ionone ring in lumirhodopsin, along with significant peptide displacement in the middle of helix III, including approximately two helical turns. This local movement results in the breaking of the electrostatic interhelical restraints mediated by many of the conserved residues among rhodopsin-like GPCRs, with consequent acquisition of full activity.

PubMed: 16908857
DOI: 10.1073/pnas.0601765103

実験手法

X-RAY DIFFRACTION (2.8 Å)