5OXU

Direct-evolutioned unspecific peroxygenase from Agrocybe aegerita

5OXU の概要

• エントリーDOI: 10.2210/pdb5oxu/pdb
• 関連するPDBエントリー: 2YOR 2YP1 5OXT
• 分子名称: Aromatic peroxygenase, PROTOPORPHYRIN IX CONTAINING FE, MAGNESIUM ION, ... (9 entities in total)
• 機能のキーワード: directed evolution, padai, unspecific peroxygenase, upo, heme-thiolate peroxidase, agrocybe aegerita, oxidoreductase
• 由来する生物種: Agrocybe aegerita (Black poplar mushroom)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38421.89

構造登録者

Ramirez-Escudero, M.,Sanz-Aparicio, J. (登録日: 2017-09-07, 公開日: 2018-12-26, 最終更新日: 2024-11-13)

主引用文献

Ramirez-Escudero, M.,Molina-Espeja, P.,Gomez de Santos, P.,Hofrichter, M.,Sanz-Aparicio, J.,Alcalde, M.
Structural Insights into the Substrate Promiscuity of a Laboratory-Evolved Peroxygenase.
Acs Chem.Biol., 13:3259-3268, 2018

PubMed Abstract: Because of their minimal requirements, substrate promiscuity and product selectivity, fungal peroxygenases are now considered to be the jewel in the crown of C-H oxyfunctionalization biocatalysts. In this work, the crystal structure of the first laboratory-evolved peroxygenase expressed by yeast was determined at a resolution of 1.5 Å. Notable differences were detected between the evolved and native peroxygenase from Agrocybe aegerita, including the presence of a full N-terminus and a broader heme access channel due to the mutations that accumulated through directed evolution. Further mutagenesis and soaking experiments with a palette of peroxygenative and peroxidative substrates suggested dynamic trafficking through the heme channel as the main driving force for the exceptional substrate promiscuity of peroxygenase. Accordingly, this study provides the first structural evidence at an atomic level regarding the mode of substrate binding for this versatile biocatalyst, which is discussed within a biological and chemical context.

PubMed: 30376293
DOI: 10.1021/acschembio.8b00500

実験手法

X-RAY DIFFRACTION (1.47 Å)