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8BVG

Bright fluorescent protein BrUSLEE with subnanosecond fluorescence lifetime

Summary for 8BVG
Entry DOI10.2210/pdb8bvg/pdb
Related4EUL
DescriptorBrUSSLEE, GLYCEROL (3 entities in total)
Functional Keywordsbrusslee, gfp-like biomarker, fluorescent protein
Biological sourceAequorea victoria (Water jellyfish, Mesonema victoria)
Total number of polymer chains6
Total formula weight160959.68
Authors
Pletnev, V.,Pletneva, N. (deposition date: 2022-12-03, release date: 2023-04-12, Last modification date: 2024-11-06)
Primary citationGoryacheva, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.38 Å)
Structure validation

248636

건을2026-02-04부터공개중

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