Mutation L232H Promotes Chromophore Maturation of EGFP-Based Fluorescent Fusion Proteins
| Autor: | M. V. Krukova, A. A. Simanovskaya, T. V. Fateeva, Alexander Popov, Galina S. Kachalova, T. V. Ivashina, Yu. S. Zeifman, Tatiana V. Rakitina |
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| Rok vydání: | 2018 |
| Předmět: |
0301 basic medicine
Mutation Chemistry Mutant Stacking General Chemistry Enhanced green fluorescent protein Chromophore Condensed Matter Physics medicine.disease_cause Fluorescence Fusion protein Green fluorescent protein 03 medical and health sciences 030104 developmental biology Biophysics medicine General Materials Science |
| Zdroj: | Crystallography Reports. 63:191-195 |
| ISSN: | 1562-689X 1063-7745 |
| Popis: | The L232H mutant of the enhanced green fluorescent protein (EGFP) was expressed and crystallized. An X-ray diffraction data set was collected from the crystals to 1.53 A resolution. An analysis of the three-dimensional structure revealed a stacking interaction between the amino-acid residues Н78 and Н232, which contributes to the fastening of the C-terminal region of the protein in the vicinity of the chromophore and influences chromophore maturation of hybrid fluorescent proteins produced by fusion of the target proteins with the C-terminus of EGFP. This hypothesis was experimentally confirmed by investigating chromophore maturation of the hybrid proteins fused to the N- and C-termini of EGFP and EGFP-L232H. |
| Databáze: | OpenAIRE |
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