5MG5
A multi-component acyltransferase PhlABC from Pseudomonas protegens soaked with the monoacetylphloroglucinol (MAPG)
Summary for 5MG5
| Entry DOI | 10.2210/pdb5mg5/pdb |
| Related | 5M3K |
| Descriptor | Hydroxymethylglutaryl-CoA synthase, 2,4-diacetylphloroglucinol biosynthesis protein, 2,4-diacetylphloroglucinol biosynthesis protein PhlC, ... (6 entities in total) |
| Functional Keywords | acyltransferase, pseudomonas protegens, phlabc, multi-component, transferase, mapg |
| Biological source | Pseudomonas protegens More |
| Total number of polymer chains | 24 |
| Total formula weight | 783538.55 |
| Authors | Pavkov-Keller, T.,Schmidt, N.G.,Kroutil, W.,Gruber, K. (deposition date: 2016-11-20, release date: 2017-12-20, Last modification date: 2024-10-09) |
| 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 Cited by 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: 30318713DOI: 10.1002/cbic.201800462 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.44 Å) |
Structure validation
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