1OXF

Expansion of the Genetic Code Enables Design of a Novel "Gold" Class of Green Fluorescent Proteins

Summary for 1OXF

• Entry DOI: 10.2210/pdb1oxf/pdb
• Related: 1EMB
• Descriptor: cyan fluorescent protein cfp (2 entities in total)
• Functional Keywords: green fluorescent protein, chromophore, amino acid incorporation, tryptophan, genetic code, luminescent protein
• Biological source: cfp marker plasmid pWM1009
• Total number of polymer chains: 1
• Total formula weight: 25554.71

Authors

Hyun Bae, J.,Rubini, M.,Jung, G.,Wiegand, G.,Seifert, M.H.,Azim, M.K.,Kim, J.S.,Zumbusch, A.,Holak, T.A.,Moroder, L.,Huber, R.,Budisa, N. (deposition date: 2003-04-02, release date: 2003-12-02, Last modification date: 2024-10-30)

Primary citation

Hyun Bae, J.,Rubini, M.,Jung, G.,Wiegand, G.,Seifert, M.H.,Azim, M.K.,Kim, J.S.,Zumbusch, A.,Holak, T.A.,Moroder, L.,Huber, R.,Budisa, N.
Expansion of the Genetic Code Enables Design of a Novel "Gold" Class of Green Fluorescent Proteins
J.Mol.Biol., 328:1071-1081, 2003

PubMed Abstract: Much effort has been dedicated to the design of significantly red shifted variants of the green fluorescent protein (GFP) from Aequoria victora (av). These approaches have been based on classical engineering with the 20 canonical amino acids. We report here an expansion of these efforts by incorporation of an amino substituted variant of tryptophan into the "cyan" GFP mutant, which turned it into a "gold" variant. This variant possesses a red shift in emission unprecedented for any avFP, similar to "red" FPs, but with enhanced stability and a very low aggregation tendency. An increasing number of non-natural amino acids are available for chromophore redesign (by engineering of the genetic code) and enable new general strategies to generate novel classes of tailor-made GFP proteins.

PubMed: 12729742
DOI: 10.1016/S0022-2836(03)00364-4

Experimental method

X-RAY DIFFRACTION (1.69 Å)