6NQL

Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-ClY)

6NQL の概要

• エントリーDOI: 10.2210/pdb6nql/pdb
• 分子名称: Fluorescent protein Dronpa, TRIETHYLENE GLYCOL (3 entities in total)
• 機能のキーワード: dronpa2, fluorescent protein
• 由来する生物種: Echinophyllia sp. SC22
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 232418.69

構造登録者

Lin, C.-Y.,Romei, M.G.,Mathews, I.I.,Boxer, S.G. (登録日: 2019-01-21, 公開日: 2019-06-12, 最終更新日: 2023-11-15)

主引用文献

Romei, M.G.,Lin, C.Y.,Mathews, I.I.,Boxer, S.G.
Electrostatic control of photoisomerization pathways in proteins.
Science, 367:76-79, 2020

PubMed Abstract: Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design.

PubMed: 31896714
DOI: 10.1126/science.aax1898

実験手法

X-RAY DIFFRACTION (2.147 Å)