6nql | pdb_00006nql

Crystal structure of fast switching M159T mutant of fluorescent protein Dronpa (Dronpa2), Y63(3-ClY)

spinqualitylabelsall models 6nql, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nql is a 8 chain structure with sequence from Echinophyllia sp. SC22. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.147Å Ligands: KZ7, PGE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5TLG6_9CNID Publication Abstract from PubMed Rotation around a specific bond after photoexcitation is central to vision and emerging opportunities in optogenetics, super-resolution microscopy, and photoactive molecular devices. Competing roles for steric and electrostatic effects that govern bond-specific photoisomerization have been widely discussed, the latter originating from chromophore charge transfer upon excitation. We systematically altered the electrostatic properties of the green fluorescent protein chromophore in a photoswitchable variant, Dronpa2, using amber suppression to introduce electron-donating and electron-withdrawing groups to the phenolate ring. Through analysis of the absorption (color), fluorescence quantum yield, and energy barriers to ground- and excited-state isomerization, we evaluate the contributions of sterics and electrostatics quantitatively and demonstrate how electrostatic effects bias the pathway of chromophore photoisomerization, leading to a generalized framework to guide protein design. Electrostatic control of photoisomerization pathways in proteins.,Romei MG, Lin CY, Mathews II, Boxer SG Science. 2020 Jan 3;367(6473):76-79. doi: 10.1126/science.aax1898. PMID:31896714 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dronpa Green Fluorescent Protein 3D structures

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