6UN4

Crystal structure of rsEGFP2, Y67(3-ClY), Y107(3-ClY)

6UN4 の概要

• エントリーDOI: 10.2210/pdb6un4/pdb
• 分子名称: Green fluorescent protein, SULFATE ION (3 entities in total)
• 機能のキーワード: photoswitchable fluorescent protein, fluorescent 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: 28697.16

構造登録者

Lin, C.-Y.,Romei, M.G.,Boxer, S.G.,Chang, J. (登録日: 2019-10-10, 公開日: 2020-07-15, 最終更新日: 2026-03-18)

主引用文献

Romei, M.G.,Lin, C.Y.,Boxer, S.G.
Structural and spectroscopic characterization of photoactive yellow protein and photoswitchable fluorescent protein constructs containing heavy atoms.
J Photochem Photobiol A Chem, 401:112738-, 2020

PubMed Abstract: Photo-induced structural rearrangements of chromophore-containing proteins are essential for various light-dependent signaling pathways and optogenetic applications. Ultrafast structural and spectroscopic methods have offered insights into these structural rearrangements across many timescales. However, questions still remain about exact mechanistic details, especially regarding photoisomerization of the chromophore within these proteins femtoseconds to picoseconds after photoexcitation. Instrumentation advancements for time-resolved crystallography and ultrafast electron diffraction provide a promising opportunity to study these reactions, but achieving enough signal-to-noise is a constant challenge. Here we present four new photoactive yellow protein constructs and one new fluorescent protein construct that contain heavy atoms either within or around the chromophore and can be expressed with high yields. Structural characterization of these constructs, most at atomic resolution, show minimal perturbation caused by the heavy atoms compared to wild-type structures. Spectroscopic studies report the effects of the heavy atom identity and location on the chromophore's photophysical properties. None of the substitutions prevent photoisomerization, although certain rates within the photocycle may be affected. Overall, these new proteins containing heavy atoms are ideal samples for state-of-theart time-resolved crystallography and electron diffraction experiments to elucidate crucial mechanistic information of photoisomerization.

PubMed: 32753830
DOI: 10.1016/j.jphotochem.2020.112738

実験手法

X-RAY DIFFRACTION (1.499 Å)