4OHS
The structure of a far-red fluorescent protein, AQ143
Summary for 4OHS
| Entry DOI | 10.2210/pdb4ohs/pdb |
| Descriptor | FAR-RED FLUORESCENT PROTEIN AQ143, CHLORIDE ION (3 entities in total) |
| Functional Keywords | far-red, beta barrel, red fluorescent protein, rfp, fluorescent protein |
| Biological source | Actinia Equina |
| Total number of polymer chains | 8 |
| Total formula weight | 213663.91 |
| Authors | Wannier, T.M.,Mayo, S.L. (deposition date: 2014-01-17, release date: 2014-02-26, Last modification date: 2014-08-06) |
| Primary citation | Wannier, T.M.,Mayo, S.L. The structure of a far-red fluorescent protein, AQ143, shows evidence in support of reported red-shifting chromophore interactions. Protein Sci., 23:1148-1153, 2014 Cited by PubMed Abstract: Engineering fluorescent proteins (FPs) to emit light at longer wavelengths is a significant focus in the development of the next generation of fluorescent biomarkers, as far-red light penetrates tissue with minimal absorption, allowing better imaging inside of biological hosts. Structure-guided design and directed evolution have led to the discovery of red FPs with significant bathochromic shifts to their emission. Here, we present the crystal structure of one of the most bathochromically shifted FPs reported to date, AQ143, a nine-point mutant of aeCP597, a chromoprotein from Actinia equina. The 2.19 Å resolution structure reveals several important chromophore interactions that contribute to the protein's far-red emission and shows dual occupancy of the green and red chromophores. PubMed: 24888769DOI: 10.1002/pro.2498 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.19 Å) |
Structure validation
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