Crystal Structure of the Aequorea victoria Green Fluorescent Protein

  title={Crystal Structure of the Aequorea victoria Green Fluorescent Protein},
  author={Mats Ormö and Andrew B. Cubitt and Karen Kallio and Larry A Gross and Roger Tsien and S. James Remington},
  pages={1392 - 1395}
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… 

Crystal structures and mutational analysis of amFP486, a cyan fluorescent protein from Anemonia majano.

The crystal structures of H199T and E150Q revealed that the stacking interaction of His-199 with the chromophore also controls the fluorescence efficiency, because the Chromophore is statistically distributed in a 1:1 ratio between cis (fluorescent) and trans (nonfluorescence) conformations.

Identification of a Fluorescent Protein from Rhacostoma Atlantica

A novel fluorescent protein from the jellyfish Rhacostoma atlantica is cloned with a somewhat unusual alanine–tyrosine–glycine amino acid sequence forms the presumed chromophore of the novel protein.

Fluorescent proteins and chromoproteins in phylum: Cnidaria

The document reviews the various proposed hypotheses on the biological functions and biochemistry of fluorescent proteins and chromoproteins, wherein a full resolution remains elusive and is the subject of on-going debate.

Special properties of green fluorescent protein-S65A.

Fluorescent proteins from nonbioluminescent Anthozoa species

We have cloned six fluorescent proteins homologous to the green fluorescent protein (GFP) from Aequorea victoria. Two of these have spectral characteristics dramatically different from GFP, emitting

Letter to the Editor: 1H, 15N and 13C backbone assignment of the Green Fluorescent Protein (GFP)

Evidence from crystallographic studies shows that the chromophore is in a deeply buried and tightly packed region within the protein core and is, therefore, excluded from solvent, which gives rise to the high fluorescence efficiency.

Defining the role of arginine 96 in green fluorescent protein fluorophore biosynthesis.

Structural, mutational, and biochemical results establish a pivotal role for the R96 positive charge in accelerating the GFP post-translational modification, with implications for peptide backbone cyclization in GFP, its homologues, and related biological systems.



Chemical structure of the hexapeptide chromophore of the Aequorea green-fluorescent protein.

The characterization of the Aequorea victoria GFP chromophore is described, which is released as a hexapeptide upon digestion of the protein with papain, formed upon cyclization of the residues Ser-dehydroTyr-Gly within the polypeptide.


Abstract— In the jellyfish Aequorea, the green‐fluorescent protein (GFP) functions as the in vivo bio‐luminescence emitter via energy transfer from the photoprotein aequorin. Accumulated evidence has

Using GFP to see the light.

  • D. Prasher
  • Biology, Chemistry
    Trends in genetics : TIG
  • 1995

Reversible denaturation of Aequorea green-fluorescent protein: physical separation and characterization of the renatured protein.

The green-fluorescent protein (GFP) that functions as a bioluminescence energy transfer acceptor in the jellyfish Aequorea has been renatured with up to 90% yield following acid, base, or guanidine

Intermolecular energy transfer in the bioluminescent system of Aequorea.

In the present study, GFP has been purified, crystallized, and partially characterized and an energy transfer in citro from aequorin to this protein has been demonstrated.