6L27
X-ray crystal structure of the mutant green fluorescent protein
Summary for 6L27
| Entry DOI | 10.2210/pdb6l27/pdb |
| Descriptor | Green fluorescent protein (2 entities in total) |
| Functional Keywords | gfp, mutant, recombinant, fluorescent protein |
| Biological source | Aequorea victoria (Jellyfish) |
| Total number of polymer chains | 1 |
| Total formula weight | 25829.03 |
| Authors | Adachi, M.,Shimizu, R.,Shibazaki, C.,Kagotani, Y.,Ostermann, A.,Schrader, T.E. (deposition date: 2019-10-02, release date: 2020-04-01, Last modification date: 2024-11-06) |
| Primary citation | Shibazaki, C.,Shimizu, R.,Kagotani, Y.,Ostermann, A.,Schrader, T.E.,Adachi, M. Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein. J Phys Chem Lett, 11:492-496, 2020 Cited by PubMed Abstract: Neutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also, the protonation states of His148 and Thr203, as well as the orientation of a critical water molecule in direct contact with the chromophore, could be determined. The results demonstrate that the deprotonated hydroxyl group in the chromophore and the nitrogen atom ND1 in His148 are charged negatively and positively, respectively, forming an ion pair. The position of the two deuterium atoms in the critical water molecule appears to be displaced slightly toward the acceptor oxygen atoms according to their omit maps. This displacement implies the formation of an intriguing electrostatic potential realized inside of the protein. Our findings provide new insights into future protein design strategies along with developments in quantum chemical calculations. PubMed: 31880458DOI: 10.1021/acs.jpclett.9b03252 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.77 Å) |
Structure validation
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