6YPI
Structure of the engineered metallo-Diels-Alderase DA7 W16G,K58Q,L77R,T78R
Summary for 6YPI
| Entry DOI | 10.2210/pdb6ypi/pdb |
| Descriptor | DA7 W16G,K58Q,L77R,T78R, ZINC ION, DI(HYDROXYETHYL)ETHER, ... (6 entities in total) |
| Functional Keywords | de novo diels-alderase, de novo protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 11426.10 |
| Authors | Basler, S.,Mori, T.,Hilvert, D. (deposition date: 2020-04-16, release date: 2021-04-28, Last modification date: 2024-06-19) |
| Primary citation | Basler, S.,Studer, S.,Zou, Y.,Mori, T.,Ota, Y.,Camus, A.,Bunzel, H.A.,Helgeson, R.C.,Houk, K.N.,Jimenez-Oses, G.,Hilvert, D. Efficient Lewis acid catalysis of an abiological reaction in a de novo protein scaffold. Nat.Chem., 13:231-235, 2021 Cited by PubMed Abstract: 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 turnovers per active site, exerts absolute control over reaction pathway and product stereochemistry, and displays a catalytic proficiency (1/K = 2.9 × 10 M) 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. PubMed: 33526894DOI: 10.1038/s41557-020-00628-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.479 Å) |
Structure validation
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