2DUE

crystal structure of a green fluorescent protein variant S65T/H148D at pH 10

2DUE の概要

• エントリーDOI: 10.2210/pdb2due/pdb
• 関連するPDBエントリー: 2DUF 2DUG 2DUH 2DUI
• 分子名称: Green fluorescent protein (2 entities in total)
• 機能のキーワード: excited state proton transfer, very short hydrogen bond, green fluorescent protein, luminescent protein
• 由来する生物種: Aequorea victoria
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26923.33

構造登録者

Shu, X.,Remington, S.J. (登録日: 2006-07-23, 公開日: 2007-07-10, 最終更新日: 2024-10-30)

主引用文献

Shu, X.,Kallio, K.,Shi, X.,Abbyad, P.,Kanchanawong, P.,Childs, W.,Boxer, S.G.,Remington, S.J.
Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 1. Mutagenesis and structural studies.
Biochemistry, 46:12005-12013, 2007

PubMed Abstract: Wild type green fluorescent protein (wt-GFP) and the variant S65T/H148D each exhibit two absorption bands, A and B, which are associated with the protonated and deprotonated chromophores, respectively. Excitation of either band leads to green emission. In wt-GFP, excitation of band A ( approximately 395 nm) leads to green emission with a rise time of 10-15 ps, due to excited-state proton transfer (ESPT) from the chromophore hydroxyl group to an acceptor. This process produces an anionic excited-state intermediate I* that subsequently emits a green photon. In the variant S65T/H148D, the A band absorbance maximum is red-shifted to approximately 415 nm, and as detailed in the accompanying papers, when the A band is excited, green fluorescence appears with a rise time shorter than the instrument time resolution ( approximately 170 fs). On the basis of the steady-state spectroscopy and high-resolution crystal structures of several variants described herein, it is proposed that in S65T/H148D, the red shift of absorption band A and the ultrafast appearance of green fluorescence upon excitation of band A are due to a very short (PubMed: 17918959
DOI: 10.1021/bi7009037

実験手法

X-RAY DIFFRACTION (1.24 Å)