6PFU

rsEGFP2 with a chlorinated chromophore in the non-fluorescent off-state in a contracted unit cell

6PFU の概要

• エントリーDOI: 10.2210/pdb6pfu/pdb
• 分子名称: Green fluorescent protein, SULFATE ION (3 entities in total)
• 機能のキーワード: green fluorescent protein, 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: 28758.77

構造登録者

Chang, J.,Romei, M.G.,Boxer, S.G. (登録日: 2019-06-22, 公開日: 2019-08-07, 最終更新日: 2023-11-15)

主引用文献

Chang, J.,Romei, M.G.,Boxer, S.G.
Structural Evidence of Photoisomerization Pathways in Fluorescent Proteins.
J.Am.Chem.Soc., 141:15504-15508, 2019

PubMed Abstract: Double-bond photoisomerization in molecules such as the green fluorescent protein (GFP) chromophore can occur either via a volume-demanding one-bond-flip pathway or via a volume-conserving hula-twist pathway. Understanding the factors that determine the pathway of photoisomerization would inform the rational design of photoswitchable GFPs as improved tools for super-resolution microscopy. In this communication, we reveal the photoisomerization pathway of a photoswitchable GFP, rsEGFP2, by solving crystal structures of and rsEGFP2 containing a monochlorinated chromophore. The position of the chlorine substituent in the state breaks the symmetry of the phenolate ring of the chromophore and allows us to distinguish the two pathways. Surprisingly, we find that the pathway depends on the arrangement of protein monomers within the crystal lattice: in a looser packing, the one-bond-flip occurs, whereas, in a tighter packing (7% smaller unit cell size), the hula-twist occurs.

PubMed: 31533429
DOI: 10.1021/jacs.9b08356

実験手法

X-RAY DIFFRACTION (1.619 Å)