1. Academic Validation
  2. Crystal structure of the Aequorea victoria green fluorescent protein

Crystal structure of the Aequorea victoria green fluorescent protein

  • Science. 1996 Sep 6;273(5280):1392-5. doi: 10.1126/science.273.5280.1392.
M Ormö 1 A B Cubitt K Kallio L A Gross R Y Tsien S J Remington
Affiliations

Affiliation

  • 1 Institute of Molecular Biology and Department of Physics, University of Oregon, Eugene, OR 97403-1226, USA.
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.

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