6PFT
rsEGFP2 with a chlorinated chromophore in the non-fluorescent off-state
Summary for 6PFT
| Entry DOI | 10.2210/pdb6pft/pdb |
| Descriptor | Green fluorescent protein, SULFATE ION (3 entities in total) |
| Functional Keywords | green fluorescent protein, fluorescent protein |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 28662.71 |
| Authors | Chang, J.,Romei, M.G.,Boxer, S.G. (deposition date: 2019-06-22, release date: 2019-08-07, Last modification date: 2023-11-15) |
| Primary citation | Chang, J.,Romei, M.G.,Boxer, S.G. Structural Evidence of Photoisomerization Pathways in Fluorescent Proteins. J.Am.Chem.Soc., 141:15504-15508, 2019 Cited by PubMed Abstract: Double-bond photoisomerization in molecules such as the green fluorescent protein (GFP) chromophore can occur either via a volume-demanding one-bond-flip pathway or via a volume-conserving hula-twist pathway. Understanding the factors that determine the pathway of photoisomerization would inform the rational design of photoswitchable GFPs as improved tools for super-resolution microscopy. In this communication, we reveal the photoisomerization pathway of a photoswitchable GFP, rsEGFP2, by solving crystal structures of and rsEGFP2 containing a monochlorinated chromophore. The position of the chlorine substituent in the state breaks the symmetry of the phenolate ring of the chromophore and allows us to distinguish the two pathways. Surprisingly, we find that the pathway depends on the arrangement of protein monomers within the crystal lattice: in a looser packing, the one-bond-flip occurs, whereas, in a tighter packing (7% smaller unit cell size), the hula-twist occurs. PubMed: 31533429DOI: 10.1021/jacs.9b08356 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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