5M3K

A multi-component acyltransferase PhlABC from Pseudomonas protegens

Summary for 5M3K

• Entry DOI: 10.2210/pdb5m3k/pdb
• Descriptor: PhlA, 2,4-diacetylphloroglucinol biosynthesis protein PhlB, 2,4-diacetylphloroglucinol biosynthesis protein PhlC, ... (5 entities in total)
• Functional Keywords: acyltransferase, pseudomonas protegens, phlabc, multi-component, transferase
• Biological source: Pseudomonas fluorescens; More
• Total number of polymer chains: 6
• Total formula weight: 195758.53

Authors

Pavkov-Keller, T.,Schmidt, N.G.,Kroutil, W.,Gruber, K. (deposition date: 2016-10-15, release date: 2017-12-20, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.83 Å)