5wx5 | pdb_00005wx5

Alkylquinolone synthase Y215V mutant from Evodia rutaecarpa

spinqualitylabelsall models 5wx5, resolution 3.06Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5wx5 is a 6 chain structure with sequence from Tetradium ruticarpum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.058Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1X8XLG0_9ROSI Publication Abstract from PubMed 2-Alkylquinolone (2AQ) alkaloids are pharmaceutically and biologically important natural products produced by both bacteria and plants, with a wide range of biological effects, including antibacterial, cytotoxic, anticholinesterase, and quorum-sensing signaling activities. These diverse activities and 2AQ occurrence in vastly different phyla have raised much interest in the biosynthesis pathways leading to their production. Previous studies in plants have suggested that type III polyketide synthases (PKSs) might be involved in 2AQ biosynthesis, but this hypothesis is untested. To this end, we cloned two novel type III polyketide synthases (PKSs), alkyldiketide-CoA synthase (ADS) and alkylquinolone synthase (AQS), from the 2AQ-producing medicinal plant, Evodia rutaecarpa (Rutaceae). Functional analyses revealed that collaboration of ADS and AQS produces 2AQ via condensations of N-methylanthraniloyl-CoA, a fatty acyl-CoA, with malonyl-CoA. We show that ADS efficiently catalyzes the decarboxylative condensation of malonyl-CoA with a fatty acyl-CoA to produce an alkyldiketide-CoA, while AQS specifically catalyzes the decarboxylative condensation of an alkyldiketide acid with N-methylanthraniloyl-CoA to generate the 2AQ scaffold via C-C/C-N bond formations. Remarkably, the ADS and AQS crystal structures at 1.80 and 2.20 A resolutions, respectively, indicated that the unique active-site architecture with Trp332 and Cys191, and the novel CoA-binding tunnel with Tyr215, principally controls the substrate and product specificities of ADS and AQS, respectively. These results provide additional insights into the catalytic versatility of the type III PKSs and their functional and evolutionary implications for 2AQ biosynthesis in plants and bacteria. 2-Alkylquinolone Alkaloid Biosynthesis in the Medicinal Plant Evodia rutaecarpa Involves Collaboration of Two Novel Type III Polyketide Synthases.,Matsui T, Kodama T, Mori T, Tadakoshi T, Noguchi H, Abe I, Morita H J Biol Chem. 2017 Apr 14. pii: jbc.M117.778977. doi: 10.1074/jbc.M117.778977. PMID:28411241 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA