5mg5

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

spinqualitylabelsall models 5mg5, resolution 3.44Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mg5 is a 24 chain structure with sequence from Pseudomonas protegens and Pseudomonas protegens Pf-5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.44Å Ligands: 13X, SCY, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q4K420_PSEF5 Publication Abstract from PubMed C-C bond forming reactions are key transformations to set up the carbon framework of organic molecules. In this context, the 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 multi-component acyltransferase from Pseudomonas protegens (PpATase) catalyzes such a Friedel-Crafts C-acylation of phenolic substrates in aqueous solution reaching up to >99% conversion without the need of CoA-activated reagents. We determined x-ray crystal structures of the native and ligand-bound complex. This multimeric enzyme consists of three subunits - PhlA, PhlB and PhlC which are arranged in a Phl(A2C2)2B4 composition. The structure of a reaction intermediate obtained from crystals soaked with the natural substrate monoacetylphloroglucinol 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 towards enhancing the substrate scope of this enzyme. Structure and catalytic mechanism of a bacterial Friedel-Crafts acylase.,Pavkov-Keller T, Schmidt NG, Zadlo-Dobrowolska A, Kroutil W, Gruber K Chembiochem. 2018 Oct 14. doi: 10.1002/cbic.201800462. PMID:30318713 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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