Crystal structure of the Aequorea victoria green fluorescent protein.
The green fluorescent protein (GFP) from the Pacific Northwest jellyfish Aequorea victoria has generated intense interest as a marker for gene expression and localization of gene products. The chromophore, resulting from the spontaneous cyclization and oxidation of the sequence -Ser65 (or Thr65)-Tyr66-Gly67-, requires the native protein fold for both formation and fluorescence emission. The structure of Thr65 GFP has been determined at 1.9 angstrom resolution. The protein fold consists of an 11-stranded beta barrel with a coaxial helix, with the chromophore forming from the central helix. Directed mutagenesis of one residue adjacent to the chromophore, Thr203, to Tyr or His results in significantly red-shifted excitation and emission maxima.
Ormö
M
M
Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, OR 97403-1226, USA.
Cubitt
A B
AB
Kallio
K
K
Gross
L A
LA
Tsien
R Y
RY
Remington
S J
SJ
D000595:Amino Acid Sequence; D018360:Crystallography, X-Ray; D049452:Green Fluorescent Proteins; D006860:Hydrogen Bonding; D008164:Luminescent Proteins / Q000737:chemistry* / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013050:Spectrometry, Fluorescence
D008164:Luminescent Proteins; D049452:Green Fluorescent Proteins