3GJ1
Non photoactivated state of PA-GFP
Summary for 3GJ1
| Entry DOI | 10.2210/pdb3gj1/pdb |
| Related | 3GJ2 |
| Descriptor | Green fluorescent protein, SULFATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | beta barrel, chromophore, luminescence, photoprotein, luminescent protein |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 4 |
| Total formula weight | 104558.20 |
| Authors | Henderson, J.N.,Gepshtein, R.,Heenan, J.R.,Kallio, K.,Huppert, D.,Remington, S.J. (deposition date: 2009-03-07, release date: 2009-03-24, Last modification date: 2024-10-16) |
| Primary citation | Henderson, J.N.,Gepshtein, R.,Heenan, J.R.,Kallio, K.,Huppert, D.,Remington, S.J. Structure and mechanism of the photoactivatable green fluorescent protein. J.Am.Chem.Soc., 131:4176-4177, 2009 Cited by PubMed Abstract: Crystal structures of the photoactivatable green fluorescent protein T203H variant (PA-GFP) have been solved in the native and photoactivated states, which under 488 nm illumination are dark and brightly fluorescent, respectively. We demonstrate that photoactivation of PA-GFP is the result of a UV-induced decarboxylation of the Glu222 side chain that shifts the chromophore equilibrium to the anionic form. Coupled with the T203H mutation, which stabilizes the native PA-GFP neutral chromophore, Glu222 decarboxylation yields a 100-fold contrast enhancement relative to wild-type GFP (WT). Additionally, the structures provide insights into the spectroscopic differences between WT and PA-GFP steady-state fluorescence maxima and excited-state proton transfer dynamics. PubMed: 19278226DOI: 10.1021/ja808851n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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