5WWK
Highly stable green fluorescent protein
Summary for 5WWK
| Entry DOI | 10.2210/pdb5wwk/pdb |
| Descriptor | Green fluorescent protein (2 entities in total) |
| Functional Keywords | chromophore modification, thermal stability fluorescence protein sensor, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 6 |
| Total formula weight | 155263.13 |
| Authors | Sriram, R.,George, A.,Kesavan, M.,Jaimohan, S.M.,Kamini, N.R.,Easwaramoorthi, S.,Ganesh, S.,Gunasekaran, K.,Ayyadurai, N. (deposition date: 2017-01-02, release date: 2017-12-13, Last modification date: 2024-10-30) |
| Primary citation | Augustine, G.,Raghavan, S.,NumbiRamudu, K.,Easwaramoorthi, S.,Shanmugam, G.,Seetharani Murugaiyan, J.,Gunasekaran, K.,Govind, C.,Karunakaran, V.,Ayyadurai, N. Excited State Electronic Interconversion and Structural Transformation of Engineered Red-Emitting Green Fluorescent Protein Mutant. J.Phys.Chem.B, 123:2316-2324, 2019 Cited by PubMed Abstract: Red fluorescent proteins with a large Stokes shift offer a limited autofluorescence background and are used in deep tissue imaging. Here, by introducing the free amino group in Aequorea victoria, the electrostatic charges of the p-hydroxybenzylidene imidazolinone chromophore of green fluorescent protein (GFP) have been altered resulting in an unusual, 85 nm red-shifted fluorescence. The structural and biophysical analysis suggested that the red shift is due to positional shift occupancy of Glu222 and Arg96, resulting in extended conjugation and a relaxed chromophore. Femtosecond transient absorption spectra exhibited that the excited state relaxation dynamics of red-shifted GFP (rGFP) (τ = 234 ps) are faster compared to the A. victoria green fluorescent protein (τ = 3.0 ns). The nanosecond time-resolved emission spectra of rGFP reveal the continuous spectral shift during emission by a solvent reorientation in the chromophore. Finally, the molecular dynamics simulations revealed the rearrangement of the hydrogen bond interactions in the chromophore vicinity, reshaping the symmetric distribution of van der Waals space to fine tune the GFP structure resulting from highly red-shifted rGFP. PubMed: 30789731DOI: 10.1021/acs.jpcb.8b10516 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.199 Å) |
Structure validation
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