6NQL
Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-ClY)
Summary for 6NQL
| Entry DOI | 10.2210/pdb6nql/pdb |
| Descriptor | Fluorescent protein Dronpa, TRIETHYLENE GLYCOL (3 entities in total) |
| Functional Keywords | dronpa2, fluorescent protein |
| Biological source | Echinophyllia sp. SC22 |
| Total number of polymer chains | 8 |
| Total formula weight | 232418.69 |
| Authors | Lin, C.-Y.,Romei, M.G.,Mathews, I.I.,Boxer, S.G. (deposition date: 2019-01-21, release date: 2019-06-12, Last modification date: 2023-11-15) |
| Primary citation | Romei, M.G.,Lin, C.Y.,Mathews, I.I.,Boxer, S.G. Electrostatic control of photoisomerization pathways in proteins. Science, 367:76-79, 2020 Cited by PubMed Abstract: Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. PubMed: 31896714DOI: 10.1126/science.aax1898 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.147 Å) |
Structure validation
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