8BVG

Bright fluorescent protein BrUSLEE with subnanosecond fluorescence lifetime

8BVG の概要

• エントリーDOI: 10.2210/pdb8bvg/pdb
• 関連するPDBエントリー: 4EUL
• 分子名称: BrUSSLEE, GLYCEROL (3 entities in total)
• 機能のキーワード: brusslee, gfp-like biomarker, fluorescent protein
• 由来する生物種: Aequorea victoria (Water jellyfish, Mesonema victoria)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 160959.68

構造登録者

Pletnev, V.,Pletneva, N. (登録日: 2022-12-03, 公開日: 2023-04-12, 最終更新日: 2024-11-06)

主引用文献

Goryacheva, E.,Efremov, R.,Krylov, N.,Artemyev, I.,Bogdanov, A.,Mamontova, A.,Pletnev, S.,Pletneva, N.,Pletnev, V.
Crystal Structure of Bright Fluorescent Protein BrUSLEE with Subnanosecond Fluorescence Lifetime; Electric and Dynamic Properties.
Int J Mol Sci, 24:-, 2023

PubMed Abstract: The rapid development of new microscopy techniques for cell biology has exposed the need for genetically encoded fluorescent tags with special properties. Fluorescent biomarkers of the same color and spectral range and different fluorescent lifetimes (FLs) became useful for fluorescent lifetime image microscopy (FLIM). One such tag, the green fluorescent protein BrUSLEE (Bright Ultimately Short Lifetime Enhanced Emitter), having an extremely short subnanosecond component of fluorescence lifetime (FL~0.66 ns) and exceptional fluorescence brightness, was designed for FLIM experiments. Here, we present the X-ray structure and discuss the structure-functional relations of BrUSLEE. Its development from the EGFP (enhanced green fluorescent proteins) precursor (FL~2.83 ns) resulted in a change of the chromophore microenvironment due to a significant alteration in the side chain conformations. To get further insight into molecular details explaining the observed differences in the photophysical properties of these proteins, we studied their structural, dynamic, and electric properties by all-atom molecular-dynamics simulations in an aqueous solution. It has been shown that compared to BrUSLEE, the mobility of the chromophore in the EGFP is noticeably limited by nonbonded interactions (mainly H-bonds) with the neighboring residues.

PubMed: 37047378
DOI: 10.3390/ijms24076403

実験手法

X-RAY DIFFRACTION (2.38 Å)