1HCJ
Photoproduct of the wild-type Aequorea victoria Green Fluorescent Protein
Summary for 1HCJ
| Entry DOI | 10.2210/pdb1hcj/pdb |
| Related | 1B9C 1BFP 1C4F 1EMB 1EMC 1EME 1EMF 1EMG 1EMK 1EML 1EMM 1F09 1F0B 1YFP 2EMD 2EMN 2EMO |
| Descriptor | GREEN FLUORESCENT PROTEIN (2 entities in total) |
| Functional Keywords | luminescent protein, fluorescent protein, beta-barrel, bioluminescence, luminescence |
| Biological source | AEQUOREA VICTORIA |
| Total number of polymer chains | 4 |
| Total formula weight | 107549.38 |
| Authors | Van Thor, J.J.,Gensch, T.,Hellingwerf, K.J.,Johnson, L. (deposition date: 2001-05-04, release date: 2001-12-07, Last modification date: 2023-12-13) |
| Primary citation | Van Thor, J.J.,Gensch, T.,Hellingwerf, K.J.,Johnson, L. Phototransformation of Green Fluorescent Protein with Uv and Visible Light Leads to Decarboxylation of Glutamate 222 Nat.Struct.Biol., 9:37-, 2002 Cited by PubMed Abstract: Wild type green fluorescent protein (GFP) from Aequorea victoria absorbs predominantly at 398 nm. Illumination with UV (254 nm) or visible (390 nm) light transforms this state (GFP(398)) into one absorbing at 483 nm (GFP(483)). Here we show that this photoconversion of GFP is a one-photon process that is paralleled by decarboxylation of Glu 222. We propose a mechanism in which decarboxylation is due to electron transfer between the gamma-carboxylate of Glu 222 and the p-hydroxybenzylidene-imidazolidinone chromophore of GFP, followed by reverse transfer of an electron and a proton to the remaining carbon side chain atom of Glu 222. Oxidative decarboxylation of a gamma-carboxylate represents a new type of posttranslational modification that may also occur in enzymes with high-potential reaction intermediates. PubMed: 11740505DOI: 10.1038/NSB739 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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