Homework 5

Crystal structure of the Aequorea victoria green fluorescent protein

Ormoe, M; Cubitt, AB; Kallio, K; Gross, LA; Tsien, RY; Remington, SJ
SCIENCE (WASH.), vol. 273, no. 5280, pp. 1392-1395, 1996

3DB file Abstract Information Rasmol Picture Blue Emission


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 -Ser super(65) (or Thr super(65))-Tyr super(66)-Gly super(67)-, requires the native protein hold for both formation and fluorescence emission. The structure of Thr super(65) 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, Thr super(203), to Tyr or His results in significantly red-shifted excitation and emission maxima.


  • PDB ID number: 1EMA
  • Expression: Plasmid: Prsetb (Invitrogen) Expression_system: Escherichia Coli Expression_system_strain: Jm109 (De3)
  • Residue number: 236
  • Number of b-sheet: 11
  • Rasmol Pictures

  • Overview
  • Chromophore(Ser65-His66-Gly67)

    Blue Emission

  • Blue Emission Variant(Y66H/Y145F):homework3
  • Picture
  • Number of helix: 4
    starting residueending residue
    GLY 4PHE 8
    TRP 57LEU 60
    GLN 69PHE 71