5MG5

A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)

5MG5 の概要

• エントリーDOI: 10.2210/pdb5mg5/pdb
• 関連するPDBエントリー: 5M3K
• 分子名称: Hydroxymethylglutaryl-CoA synthase, 2,4-diacetylphloroglucinol biosynthesis protein, 2,4-diacetylphloroglucinol biosynthesis protein PhlC, ... (6 entities in total)
• 機能のキーワード: acyltransferase, pseudomonas protegens, phlabc, multi-component, transferase, mapg
• 由来する生物種: Pseudomonas protegens; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 783538.55

構造登録者

Pavkov-Keller, T.,Schmidt, N.G.,Kroutil, W.,Gruber, K. (登録日: 2016-11-20, 公開日: 2017-12-20, 最終更新日: 2024-10-09)

主引用文献

Pavkov-Keller, T.,Schmidt, N.G.,Zadlo-Dobrowolska, A.,Kroutil, W.,Gruber, K.
Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.
Chembiochem, 20:88-95, 2019

PubMed Abstract: C-C bond-forming reactions are key transformations for setting up the carbon frameworks of organic compounds. In this context, Friedel-Crafts acylation is commonly used for the synthesis of aryl ketones, which are common motifs in many fine chemicals and natural products. A bacterial multicomponent acyltransferase from Pseudomonas protegens (PpATase) catalyzes such Friedel-Crafts C-acylation of phenolic substrates in aqueous solution, reaching up to >99 % conversion without the need for CoA-activated reagents. We determined X-ray crystal structures of the native and ligand-bound complexes. This multimeric enzyme consists of three subunits: PhlA, PhlB, and PhlC, arranged in a Phl(A C ) B composition. The structure of a reaction intermediate obtained from crystals soaked with the natural substrate 1-(2,4,6-trihydroxyphenyl)ethanone together with site-directed mutagenesis studies revealed that only residues from the PhlC subunits are involved in the acyl transfer reaction, with Cys88 very likely playing a significant role during catalysis. These structural and mechanistic insights form the basis of further enzyme engineering efforts directed towards enhancing the substrate scope of this enzyme.

PubMed: 30318713
DOI: 10.1002/cbic.201800462

実験手法

X-RAY DIFFRACTION (3.44 Å)