|1gfl, resolution 1.90Å ()|
STRUCTURE OF GREEN FLUORESCENT PROTEIN
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.
The molecular structure of green fluorescent protein., Yang F, Moss LG, Phillips GN Jr, Nat Biotechnol. 1996 Oct;14(10):1246-51. PMID:9631087
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1gfl is a 2 chain structure with sequence from Aequorea victoria. The June 2003 RCSB PDB Molecule of the Month feature on Green Fluorescent Protein (GFP) by David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_6. Full crystallographic information is available from OCA.
- Alyssa Marsico/Sandbox 1
- Devon McCarthy/Sandbox 1
- Green Fluorescent Protein
- Green Fluorescent Protein: Research Tool
- User:Joanne Lau/Sandbox 5