2G6Y

Crystal structure of the novel green fluorescent protein from marine copepod Pontellina plumata

Summary for 2G6Y

• Entry DOI: 10.2210/pdb2g6y/pdb
• Related: 2G6X
• Descriptor: green fluorescent protein 2 (2 entities in total)
• Functional Keywords: green fluorescent protein, natural chromophore, rapid maturation, beta-can, luminescent protein
• Biological source: Pontellina plumata
• Total number of polymer chains: 4
• Total formula weight: 97576.69

Authors

Evdokimov, A.G.,Pokross, M.E.,Chudakov, D.M. (deposition date: 2006-02-26, release date: 2006-03-28, Last modification date: 2024-10-30)

Primary citation

Evdokimov, A.G.,Pokross, M.E.,Egorov, N.S.,Zaraisky, A.G.,Yampolsky, I.V.,Merzlyak, E.M.,Shkoporov, A.N.,Sander, I.,Lukyanov, K.A.,Chudakov, D.M.
Structural basis for the fast maturation of Arthropoda green fluorescent protein.
Embo Rep., 7:1006-1012, 2006

PubMed Abstract: Since the cloning of Aequorea victoria green fluorescent protein (GFP) in 1992, a family of known GFP-like proteins has been growing rapidly. Today, it includes more than a hundred proteins with different spectral characteristics cloned from Cnidaria species. For some of these proteins, crystal structures have been solved, showing diversity in chromophore modifications and conformational states. However, we are still far from a complete understanding of the origin, functions and evolution of the GFP family. Novel proteins of the family were recently cloned from evolutionarily distant marine Copepoda species, phylum Arthropoda, demonstrating an extremely rapid generation of fluorescent signal. Here, we have generated a non-aggregating mutant of Copepoda fluorescent protein and solved its high-resolution crystal structure. It was found that the protein beta-barrel contains a pore, leading to the chromophore. Using site-directed mutagenesis, we showed that this feature is critical for the fast maturation of the chromophore.

PubMed: 16936637
DOI: 10.1038/sj.embor.7400787

Experimental method

X-RAY DIFFRACTION (1.6 Å)