8xyn

Structure of the engineered retro-aldolase RA95.5-8

spinqualitylabelsall models 8xyn, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8xyn is a 2 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: A1LXX Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The introduction of an abiological catalytic group into the binding pocket of a protein host allows for the expansion of enzyme chemistries. Here, we report the generation of an artificial enzyme by genetic encoding of a non-canonical amino acid that contains a secondary amine side chain. The non-canonical amino acid and the binding pocket function synergistically to catalyze the asymmetric nitrocyclopropanation of alpha,beta-unsaturated aldehydes by the iminium activation mechanism. The designer enzyme was evolved to an optimal variant that catalyzes the reaction at high conversions with high diastereo- and enantioselectivity. This work demonstrates the application of genetic code expansion in enzyme design and expands the scope of enzyme-catalyzed abiological reactions. An Artificial Enzyme for Asymmetric Nitrocyclopropanation of alpha,beta-Unsaturated Aldehydes-Design and Evolution.,Yu MZ, Yuan Y, Li ZJ, Kunthic T, Wang HX, Xu C, Xiang Z Angew Chem Int Ed Engl. 2024 Jun 17;63(25):e202401635. doi: , 10.1002/anie.202401635. Epub 2024 May 14. PMID:38597773 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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