7BWW

Structure of the engineered metallo-Diels-Alderase DA7 W16S

7BWW の概要

• エントリーDOI: 10.2210/pdb7bww/pdb
• 分子名称: metallo-Diels-Alderase DA7 W16S, BENZOIC ACID, PENTAETHYLENE GLYCOL, ... (7 entities in total)
• 機能のキーワード: de novo diels-alderase, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 44360.74

構造登録者

Basler, S.,Mori, T.,Hilvert, D. (登録日: 2020-04-16, 公開日: 2021-04-21, 最終更新日: 2023-11-29)

主引用文献

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

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: 33526894
DOI: 10.1038/s41557-020-00628-4

実験手法

X-RAY DIFFRACTION (1.5 Å)