Premium
Structural basis for the fast maturation of Arthropoda green fluorescent protein
Author(s) -
Evdokimov Artem G,
Pokross Matthew E,
Egorov Nikolay S,
Zaraisky Andrey G,
Yampolsky Ilya V,
Merzlyak Ekaterina M,
Shkoporov Andrey N,
Sander Ian,
Lukyanov Konstantin A,
Chudakov Dmitriy M
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400787
Subject(s) - green fluorescent protein , aequorea victoria , biology , chromophore , fluorescence , mutagenesis , mutant , genetics , gene , chemistry , physics , organic chemistry , quantum mechanics
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 β‐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.