4P1Q
GREEN FLUORESCENT PROTEIN E222H VARIANT
Summary for 4P1Q
| Entry DOI | 10.2210/pdb4p1q/pdb |
| Descriptor | Green fluorescent protein, SODIUM ION (3 entities in total) |
| Functional Keywords | chromophore, beta-barrel, luminescence, photoprotein, bioluminescence, fluorescent protein, luminescent protein |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 25845.95 |
| Authors | Klein, M.,Carius, Y.,Auerbach, D.,Franz, S.,Jung, G.,Lancaster, C.R.D. (deposition date: 2014-02-27, release date: 2014-07-16, Last modification date: 2024-11-06) |
| Primary citation | Auerbach, D.,Klein, M.,Franz, S.,Carius, Y.,Lancaster, C.R.,Jung, G. Replacement of Highly Conserved E222 by the Photostable Non-photoconvertible Histidine in GFP. Chembiochem, 15:1404-1408, 2014 Cited by PubMed Abstract: The widely used green fluorescent protein (GFP) decarboxylates upon irradiation; this involves removal of the acidic function of the glutamic acid at position 222, thereby resulting in the irreversible photoconversion of GFP. To suppress this phenomenon, the photostable, non-photoconvertible histidine was introduced at position 222 in GFP. The variant E222H shows negligible photodynamic processes and high expression yield. In addition, the stable and bright fluorescence over a wide pH range makes the E222H protein an alternative for GFP in fluorescence imaging and spectroscopy. Other fluorescent proteins are predicted to benefit from replacement of the catalytic glutamic acid by histidine. PubMed: 24919579DOI: 10.1002/cbic.201402075 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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