7ZCA

Crystal structure of the F191M/F201A variant of Variovorax paradoxus indole monooxygenase (VpIndA1) in complex with benzyl phenyl sulfoxide

7ZCA の概要

• エントリーDOI: 10.2210/pdb7zca/pdb
• 分子名称: Putative dehydrogenase/oxygenase subunit (Flavoprotein), phenylsulfinylmethylbenzene, FLAVIN-ADENINE DINUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: fad-dependent monooxygenase, styrene monooxygenase, stya1, imo, oxidoreductase
• 由来する生物種: Variovorax paradoxus EPS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48509.69

構造登録者

Kratky, J.,Weisse, R.,Strater, N. (登録日: 2022-03-26, 公開日: 2023-02-22, 最終更新日: 2024-02-07)

主引用文献

Kratky, J.,Eggerichs, D.,Heine, T.,Hofmann, S.,Sowa, P.,Weisse, R.H.,Tischler, D.,Strater, N.
Structural and Mechanistic Studies on Substrate and Stereoselectivity of the Indole Monooxygenase VpIndA1: New Avenues for Biocatalytic Epoxidations and Sulfoxidations.
Angew.Chem.Int.Ed.Engl., 62:e202300657-e202300657, 2023

PubMed Abstract: Flavoprotein monooxygenases are a versatile group of enzymes for biocatalytic transformations. Among these, group E monooxygenases (GEMs) catalyze enantioselective epoxidation and sulfoxidation reactions. Here, we describe the crystal structure of an indole monooxygenase from the bacterium Variovorax paradoxus EPS, a GEM designated as VpIndA1. Complex structures with substrates reveal productive binding modes that, in conjunction with force-field calculations and rapid mixing kinetics, reveal the structural basis of substrate and stereoselectivity. Structure-based redesign of the substrate cavity yielded variants with new substrate selectivity (for sulfoxidation of benzyl phenyl sulfide) or with greatly enhanced stereoselectivity (from 35.1 % to 99.8 % ee for production of (1S,2R)-indene oxide). This first determination of the substrate binding mode of GEMs combined with structure-function relationships opens the door for structure-based design of these powerful biocatalysts.

PubMed: 36762980
DOI: 10.1002/anie.202300657

実験手法

X-RAY DIFFRACTION (1.68 Å)