1GFL
STRUCTURE OF GREEN FLUORESCENT PROTEIN
Summary for 1GFL
| Entry DOI | 10.2210/pdb1gfl/pdb |
| Descriptor | GREEN FLUORESCENT PROTEIN (2 entities in total) |
| Functional Keywords | fluorophore green fluorescent protein, luminescence, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 2 |
| Total formula weight | 53782.54 |
| Authors | Yang, F.,Moss, L.G.,Phillips Jr., G.N. (deposition date: 1996-08-23, release date: 1997-01-11, Last modification date: 2024-10-23) |
| Primary citation | Yang, F.,Moss, L.G.,Phillips Jr., G.N. The molecular structure of green fluorescent protein. Nat.Biotechnol., 14:1246-1251, 1996 Cited by PubMed Abstract: The crystal structure of recombinant wild-type green fluorescent protein (GFP) has been solved to a resolution of 1.9 A by multiwavelength anomalous dispersion phasing methods. The protein is in the shape of a cylinder, comprising 11 strands of beta-sheet with an alpha-helix inside and short helical segments on the ends of the cylinder. This motif, with beta-structure on the outside and alpha-helix on the inside, represents a new protein fold, which we have named the beta-can. Two protomers pack closely together to form a dimer in the crystal. The fluorophores are protected inside the cylinders, and their structures are consistent with the formation of aromatic systems made up of Tyr66 with reduction of its C alpha-C beta bond coupled with cyclization of the neighboring glycine and serine residues. The environment inside the cylinder explains the effects of many existing mutants of GFP and suggests specific side chains that could be modified to change the spectral properties of GFP. Furthermore, the identification of the dimer contacts may allow mutagenic control of the state of assembly of the protein. PubMed: 9631087DOI: 10.1038/nbt1096-1246 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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