6JGJ

Crystal structure of the F99S/M153T/V163A/E222Q variant of GFP at 0.78 A

6JGJ の概要

• エントリーDOI: 10.2210/pdb6jgj/pdb
• 分子名称: Green fluorescent protein, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: green fluorescent protein, hydrogen, fluorescent protein
• 由来する生物種: Aequorea victoria (Jellyfish)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25891.58

構造登録者

Takaba, K.,Tai, Y.,Hanazono, Y.,Miki, K.,Takeda, K. (登録日: 2019-02-14, 公開日: 2019-04-17, 最終更新日: 2024-10-23)

主引用文献

Takaba, K.,Tai, Y.,Eki, H.,Dao, H.A.,Hanazono, Y.,Hasegawa, K.,Miki, K.,Takeda, K.
Subatomic resolution X-ray structures of green fluorescent protein.
Iucrj, 6:387-400, 2019

PubMed Abstract: Green fluorescent protein (GFP) is a light-emitting protein that does not require a prosthetic group for its fluorescent activity. As such, GFP has become indispensable as a molecular tool in molecular biology. Nonetheless, there has been no subatomic elucidation of the GFP structure owing to the structural polymorphism around the chromophore. Here, subatomic resolution X-ray structures of GFP without the structural polymorphism are reported. The positions of H atoms, hydrogen-bonding network patterns and accurate geometric parameters were determined for the two protonated forms. Compared with previously determined crystal structures and theoretically optimized structures, the anionic chromophores of the structures represent the authentic resonance state of GFP. In addition, charge-density analysis based on atoms-in-molecules theory and noncovalent interaction analysis highlight weak but substantial interactions between the chromophore and the protein environment. Considered with the derived chemical indicators, the lone pair-π interactions between the chromophore and Thr62 should play a sufficient role in maintaining the electronic state of the chromophore. These results not only reveal the fine structural features that are critical to understanding the properties of GFP, but also highlight the limitations of current quantum-chemical calculations.

PubMed: 31098020
DOI: 10.1107/S205225251900246X

実験手法

X-RAY DIFFRACTION (0.78 Å)