1YFP
STRUCTURE OF YELLOW-EMISSION VARIANT OF GFP
Summary for 1YFP
Entry DOI | 10.2210/pdb1yfp/pdb |
Descriptor | YELLOW FLUORESCENT PROTEIN (2 entities in total) |
Functional Keywords | luminescence, green fluorescent protein, yellow-emission variant, bioluminescence, photoactive protein, fluorescent tag |
Biological source | Aequorea victoria |
Total number of polymer chains | 2 |
Total formula weight | 51419.99 |
Authors | Wachter, R.M.,Elsliger, M.-A.,Kallio, K.,Hanson, G.T.,Remington, S.J. (deposition date: 1998-08-28, release date: 1998-10-28, Last modification date: 2024-10-16) |
Primary citation | Wachter, R.M.,Elsliger, M.A.,Kallio, K.,Hanson, G.T.,Remington, S.J. Structural basis of spectral shifts in the yellow-emission variants of green fluorescent protein. Structure, 6:1267-1277, 1998 Cited by PubMed Abstract: Because of its ability to spontaneously generate its own fluorophore, the green fluorescent protein (GFP) from the jellyfish Aequorea victoria is used extensively as a fluorescent marker in molecular and cell biology. The yellow fluorescent proteins (YFPs) have the longest wavelength emissions of all GFP variants examined to date. This shift in the spectrum is the result of a T203Y substitution (single-letter amino acid code), a mutation rationally designed on the basis of the X-ray structure of GFP S65T. PubMed: 9782051DOI: 10.1016/S0969-2126(98)00127-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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