5F6Z
Sandercyanin Fluorescent Protein purified from Sander vitreus
Summary for 5F6Z
| Entry DOI | 10.2210/pdb5f6z/pdb |
| Related | 5EZ2 |
| Descriptor | Sandercyanin Fluorescent Protein, BILIVERDINE IX ALPHA, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | sandercyanin fluorescent protein (sfp), walleye, lipocalin, photo-stability, red fluorescent protein, fluorescent protein |
| Biological source | Sander vitreus |
| Total number of polymer chains | 4 |
| Total formula weight | 77398.93 |
| Authors | Ghosh, S.,Yu, C.L.,Ferraro, D.,Sudha, S.,Pal, S.,Schaefer, W.,Gibson, D.T.,Subramanian, R. (deposition date: 2015-12-07, release date: 2016-09-28, Last modification date: 2024-11-06) |
| Primary citation | Ghosh, S.,Yu, C.L.,Ferraro, D.J.,Sudha, S.,Pal, S.K.,Schaefer, W.F.,Gibson, D.T.,Ramaswamy, S. Blue protein with red fluorescence Proc.Natl.Acad.Sci.USA, 113:11513-11518, 2016 Cited by PubMed Abstract: The walleye (Sander vitreus) is a golden yellow fish that inhabits the Northern American lakes. The recent sightings of the blue walleye and the correlation of its sighting to possible increased UV radiation have been proposed earlier. The underlying molecular basis of its adaptation to increased UV radiation is the presence of a protein (Sandercyanin)-ligand complex in the mucus of walleyes. Degradation of heme by UV radiation results in the formation of Biliverdin IXα (BLA), the chromophore bound to Sandercyanin. We show that Sandercyanin is a monomeric protein that forms stable homotetramers on addition of BLA to the protein. A structure of the Sandercyanin-BLA complex, purified from the fish mucus, reveals a glycosylated protein with a lipocalin fold. This protein-ligand complex absorbs light in the UV region (λ of 375 nm) and upon excitation at this wavelength emits in the red region (λ of 675 nm). Unlike all other known biliverdin-bound fluorescent proteins, the chromophore is noncovalently bound to the protein. We provide here a molecular rationale for the observed spectral properties of Sandercyanin. PubMed: 27688756DOI: 10.1073/pnas.1525622113 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.248 Å) |
Structure validation
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