8AM4
Cl-rsEGFP2 Long Wavelength Structure
Summary for 8AM4
| Entry DOI | 10.2210/pdb8am4/pdb |
| Descriptor | Green fluorescent protein (1 entity in total) |
| Functional Keywords | gfp-like protein, beta-barrel, bioluminescence, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 28566.65 |
| Authors | Orr, C.M.,Fadini, A.,van Thor, J. (deposition date: 2022-08-02, release date: 2023-08-02, Last modification date: 2024-01-31) |
| Primary citation | Fadini, A.,Hutchison, C.D.M.,Morozov, D.,Chang, J.,Maghlaoui, K.,Perrett, S.,Luo, F.,Kho, J.C.X.,Romei, M.G.,Morgan, R.M.L.,Orr, C.M.,Cordon-Preciado, V.,Fujiwara, T.,Nuemket, N.,Tosha, T.,Tanaka, R.,Owada, S.,Tono, K.,Iwata, S.,Boxer, S.G.,Groenhof, G.,Nango, E.,van Thor, J.J. Serial Femtosecond Crystallography Reveals that Photoactivation in a Fluorescent Protein Proceeds via the Hula Twist Mechanism. J.Am.Chem.Soc., 2023 Cited by PubMed Abstract: Chromophore photoisomerization is a fundamental process in chemistry and in the activation of many photosensitive proteins. A major task is understanding the effect of the protein environment on the efficiency and direction of this reaction compared to what is observed in the gas and solution phases. In this study, we set out to visualize the hula twist (HT) mechanism in a fluorescent protein, which is hypothesized to be the preferred mechanism in a spatially constrained binding pocket. We use a chlorine substituent to break the twofold symmetry of the embedded phenolic group of the chromophore and unambiguously identify the HT primary photoproduct. Through serial femtosecond crystallography, we then track the photoreaction from femtoseconds to the microsecond regime. We observe signals for the photoisomerization of the chromophore as early as 300 fs, obtaining the first experimental structural evidence of the HT mechanism in a protein on its femtosecond-to-picosecond timescale. We are then able to follow how chromophore isomerization and twisting lead to secondary structure rearrangements of the protein β-barrel across the time window of our measurements. PubMed: 37418747DOI: 10.1021/jacs.3c02313 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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