1EMA

GREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA

Summary for 1EMA

• Entry DOI: 10.2210/pdb1ema/pdb
• Descriptor: GREEN FLUORESCENT PROTEIN (2 entities in total)
• Functional Keywords: beta-barrel, autocatalytic, fluorophore, bioluminescense fluorescent protein, fluorescent protein
• Biological source: Aequorea victoria
• Total number of polymer chains: 1
• Total formula weight: 27226.75

Authors

Ormo, M.,Remington, S.J. (deposition date: 1996-08-01, release date: 1996-11-08, Last modification date: 2024-10-23)

Primary citation

Ormo, M.,Cubitt, A.B.,Kallio, K.,Gross, L.A.,Tsien, R.Y.,Remington, S.J.
Crystal structure of the Aequorea victoria green fluorescent protein.
Science, 273:1392-1395, 1996

PubMed Abstract: 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.

PubMed: 8703075

Experimental method

X-RAY DIFFRACTION (1.9 Å)