7ouc

Crystal structure of the flavoprotein monooxygenase GrhO5 from griseorhodin A biosynthesis

spinqualitylabelsall models 7ouc, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7ouc is a 1 chain structure with sequence from Streptomyces sp. JP95. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å Ligands: FAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8KSX7_9ACTN Publication Abstract from PubMed The medically important bacterial aromatic polyketide natural products typically feature a planar, polycyclic core structure. An exception is found for the rubromycins, whose backbones are disrupted by a bisbenzannulated [5,6]-spiroketal pharmacophore that was recently shown to be assembled by flavin-dependent enzymes. In particular, a flavoprotein monooxygenase proved critical for the drastic oxidative rearrangement of a pentangular precursor and the installment of an intermediate [6,6]-spiroketal moiety. Here we provide structural and mechanistic insights into the control of catalysis by this spiroketal synthase, which fulfills several important functions as reductase, monooxygenase, and presumably oxidase. The enzyme hereby tightly controls the redox state of the substrate to counteract shunt product formation, while also steering the cleavage of three carbon-carbon bonds. Our work illustrates an exceptional strategy for the biosynthesis of stable chroman spiroketals. Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.,Teufel R, Toplak M, Saleem-Batcha R, Piel J Angew Chem Int Ed Engl. 2021 Oct 15. doi: 10.1002/anie.202109384. PMID:34652045 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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