9C74
superfolder Green Fluorescent Protein with meta-nitro-tyrosine incorporated at position 66
Summary for 9C74
| Entry DOI | 10.2210/pdb9c74/pdb |
| Related | 6UN6 |
| Descriptor | Green fluorescent protein, SODIUM ION (3 entities in total) |
| Functional Keywords | nitrotyrosine, gfp, sfgfp, uaa, ncaa, fluorescent protein |
| Biological source | Aequorea victoria |
| Total number of polymer chains | 1 |
| Total formula weight | 27127.41 |
| Authors | Phillips-Piro, C.M.,Broughton, D.P. (deposition date: 2024-06-10, release date: 2024-10-16, Last modification date: 2024-10-30) |
| Primary citation | Broughton, D.P.,Holod, C.G.,Camilo-Contreras, A.,Harris, D.R.,Brewer, S.H.,Phillips-Piro, C.M. Modulating the pH dependent photophysical properties of green fluorescent protein. Rsc Adv, 14:32284-32291, 2024 Cited by PubMed Abstract: The photophysical properties of the β-barrel superfolder green fluorescent protein (sfGFP) arise from the chromophore that forms post-translationally in the interior of the protein. Specifically, the protonation state of the side chain of tyrosine 66 in the chromophore, in addition to the network of hydrogen bonds between the chromophore and surrounding residues, is directly related to the electronic absorbance and emission properties of the protein. The pH dependence of the photophysical properties of this protein were modulated by the genetic, site-specific incorporation of 3-nitro-l-tyrosine (mNOY) at site 66 in sfGFP. The altered photophysical properties of this noncanonical amino acid (ncAA) sfGFP construct were assessed by absorbance and fluorescence spectroscopies. Notably, a comparison of the p of the 3-nitrophenol side chain of mNOY incorporated in the protein relative to the phenol side chain of the tyrosine at site 66 in the native chromophore as well as the p of the 3-nitrophenol side chain of the free ncAA were measured and are compared. A structural analysis of the ncAA containing sfGFP construct is presented to yield molecular insight into the origin of the altered absorbance and fluorescence properties of the protein. PubMed: 39421683DOI: 10.1039/d4ra05058d PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.51 Å) |
Structure validation
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