2Z6Y

Crystal structure of a photoswitchable GFP-like protein Dronpa in the bright-state

2Z6Y の概要

• エントリーDOI: 10.2210/pdb2z6y/pdb
• 関連するPDBエントリー: 2Z1O 2Z6X 2Z6Z
• 分子名称: Fluorescent protein Dronpa (2 entities in total)
• 機能のキーワード: gfp-like protein, photochromism, fluorescent protein
• 由来する生物種: Echinophyllia sp. SC22
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 103120.72

構造登録者

Kikuchi, A.,Jeyakanthan, J.,Taka, J.,Shiro, Y.,Mizuno, H.,Miyawaki, A. (登録日: 2007-08-09, 公開日: 2008-07-22, 最終更新日: 2024-11-06)

主引用文献

Mizuno, H.,Mal, T.K.,Walchli, M.,Kikuchi, A.,Fukano, T.,Ando, R.,Jeyakanthan, J.,Taka, J.,Shiro, Y.,Ikura, M.,Miyawaki, A.
Light-dependent regulation of structural flexibility in a photochromic fluorescent protein.
Proc.Natl.Acad.Sci.Usa, 105:9227-9232, 2008

PubMed Abstract: The structural basis for the photochromism in the fluorescent protein Dronpa is poorly understood, because the crystal structures of the bright state of the protein did not provide an answer to the mechanism of the photochromism, and structural determination of the dark state has been elusive. We performed NMR analyses of Dronpa in solution at ambient temperatures to find structural flexibility of the protein in the dark state. Light-induced changes in interactions between the chromophore and beta-barrel are responsible for switching between the two states. In the bright state, the apex of the chromophore tethers to the barrel by a hydrogen bond, and an imidazole ring protruding from the barrel stabilizes the plane of the chromophore. These interactions are disrupted by strong illumination with blue light, and the chromophore, together with a part of the beta-barrel, becomes flexible, leading to a nonradiative decay process.

PubMed: 18574155
DOI: 10.1073/pnas.0709599105

実験手法

X-RAY DIFFRACTION (2 Å)