7bww | pdb_00007bww

Structure of the engineered metallo-Diels-Alderase DA7 W16S

spinqualitylabelsall models 7bww, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bww is a 4 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 1.5Å Ligands: 1PE, ACY, BEZ, PEG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed New enzyme catalysts are usually engineered by repurposing the active sites of natural proteins. Here we show that design and directed evolution can be used to transform a non-natural, functionally naive zinc-binding protein into a highly active catalyst for an abiological hetero-Diels-Alder reaction. The artificial metalloenzyme achieves >10(4) turnovers per active site, exerts absolute control over reaction pathway and product stereochemistry, and displays a catalytic proficiency (1/KTS = 2.9 x 10(10) M(-1)) that exceeds all previously characterized Diels-Alderases. These properties capitalize on effective Lewis acid catalysis, a chemical strategy for accelerating Diels-Alder reactions common in the laboratory but so far unknown in nature. Extension of this approach to other metal ions and other de novo scaffolds may propel the design field in exciting new directions. Efficient Lewis acid catalysis of an abiological reaction in a de novo protein scaffold.,Basler S, Studer S, Zou Y, Mori T, Ota Y, Camus A, Bunzel HA, Helgeson RC, Houk KN, Jimenez-Oses G, Hilvert D Nat Chem. 2021 Mar;13(3):231-235. doi: 10.1038/s41557-020-00628-4. Epub 2021 Feb , 1. PMID:33526894 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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