7rrj | pdb_00007rrj

Crystal structure of fast switching M159Q mutant of fluorescent protein Dronpa (Dronpa2)

spinqualitylabelsall models 7rrj, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7rrj 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 2.2Å Ligands: GYC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5TLG6_9CNID Publication Abstract from PubMed The past decades have witnessed an explosion of de novo protein designs with a remarkable range of scaffolds. It remains challenging, however, to design catalytic functions that are competitive with naturally occurring counterparts as well as biomimetic or nonbiological catalysts. Although directed evolution often offers efficient solutions, the fitness landscape remains opaque. Green fluorescent protein (GFP), which has revolutionized biological imaging and assays, is one of the most redesigned proteins. While not an enzyme in the conventional sense, GFPs feature competing excited-state decay pathways with the same steric and electrostatic origins as conventional ground-state catalysts, and they exert exquisite control over multiple reaction outcomes through the same principles. Thus, GFP is an "excited-state enzyme". Herein we show that rationally designed mutants and hybrids that contain environmental mutations and substituted chromophores provide the basis for a quantitative model and prediction that describes the influence of sterics and electrostatics on excited-state catalysis of GFPs. As both perturbations can selectively bias photoisomerization pathways, GFPs with fluorescence quantum yields (FQYs) and photoswitching characteristics tailored for specific applications could be predicted and then demonstrated. The underlying energetic landscape, readily accessible via spectroscopy for GFPs, offers an important missing link in the design of protein function that is generalizable to catalyst design. Energetic Basis and Design of Enzyme Function Demonstrated Using GFP, an Excited-State Enzyme.,Lin CY, Romei MG, Mathews II, Boxer SG J Am Chem Soc. 2022 Mar 9;144(9):3968-3978. doi: 10.1021/jacs.1c12305. Epub 2022 , Feb 24. PMID:35200017 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Dronpa

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