6l26

Neutron crystal structure of the mutant green fluorescent protein (EGFP)

spinqualitylabelsall models 6l26, resolution 1.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6l26 is a 1 chain structure with sequence from Nicotiana benthamiana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Neutron Diffraction, Resolution 1.444Å Ligands: CRO, D3O, DOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W6KDG8_NICBE Publication Abstract from PubMed 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. Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.,Shibazaki C, Shimizu R, Kagotani Y, Ostermann A, Schrader TE, Adachi M J Phys Chem Lett. 2020 Jan 16;11(2):492-496. doi: 10.1021/acs.jpclett.9b03252., Epub 2020 Jan 6. PMID:31880458 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Green Fluorescent Protein 3D structures

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