9qm2

Crystal Structure of the flavoprotein monooxygenase RslO9 from Streptomyces bottropensis

spinqualitylabelsall models 9qm2, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9qm2 is a 1 chain structure with sequence from Streptomyces bottropensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CL, FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8QLE8_9ACTN Publication Abstract from PubMed Aromatic polyketides from Actinobacteria are structurally complex bioactive natural products with significant therapeutic potential, whose biosynthesis involves polyketide chain assembly, keto reduction, cyclization, and aromatization. This is followed by pathway-specific enzymatic tailoring steps, occasionally including rare oxidative rearrangements of the carbon skeleton, as exemplified by the rishirilides. In this study, we investigate RslO9, a flavin-dependent tailoring key enzyme of rishirilide biosynthesis, previously hypothesized to facilitate a lactone-forming Baeyer-Villiger oxidation of the rishirilide naphthoquinone core and subsequent intramolecular aldol condensation. Through detailed investigation of RslO9's mechanism, structural features, and substrate scope, we unexpectedly found that the naphthoquinone moiety of the non-natural substrate lapachol undergoes hydroxylation followed by a benzilic acid rearrangement, producing the Hooker intermediate-a hallmark of the intricate Hooker oxidation. Our data support a similar alkyl migration mechanism for RslO9's native substrate, upending its prior classification as a Baeyer-Villiger monooxygenase and challenging the proposed role of related enzymes while also providing a novel framework for exploring their catalytic roles. A Hooker Oxygenase Archetype in Polyketide Biosynthesis Challenging the Baeyer-Villiger Monooxygenase Paradigm.,Weddeling HG, Sowa ST, Bialas E, Reese S, Merten C, Lill M, Bechthold A, Teufel R J Am Chem Soc. 2026 Jan 26. doi: 10.1021/jacs.5c21759. PMID:41588612 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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