Structural basis for the fast maturation of Arthropoda green fluorescent protein
| Autor: | Andrey G. Zaraisky, Dmitriy M. Chudakov, Ilya V Yampolsky, Andrey N. Shkoporov, Matthew Pokross, Konstantin A. Lukyanov, Artem G. Evdokimov, Nikolay S Egorov, Ekaterina M. Merzlyak, Ian M. Sander |
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| Jazyk: | angličtina |
| Rok vydání: | 2006 |
| Předmět: |
Models
Molecular Protein Folding Embryo Nonmammalian Protein Conformation Recombinant Fusion Proteins Mutant Scientific Report Green Fluorescent Proteins Mutagenesis (molecular biology technique) Crystallography X-Ray Biochemistry Green fluorescent protein Copepoda Xenopus laevis Genetics Animals Humans Molecular Biology Arthropods Cloning biology Phylum Chromophore biology.organism_classification Fluorescence Cell biology Protein Structure Tertiary Structural Homology Protein Protein Biosynthesis Aequorea victoria HeLa Cells |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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