6da6

Crystal structure of the TtnD decarboxylase from the tautomycetin biosynthesis pathway of Streptomyces griseochromogenes, apo form at 2.6 A resolution (P212121)

spinqualitylabelsall models 6da6, resolution 2.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6da6 is a 4 chain structure with sequence from Streptomyces griseochromogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.59Å Ligands: GOL, MG, UNL Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C6ZCR8_9ACTN Catalyzes the reversible decarboxylation of aromatic carboxylic acids.[HAMAP-Rule:MF_01983] Publication Abstract from PubMed Tautomycetin (TTN) is a polyketide natural product featuring a terminal alkene. Functional characterization of the genes within the ttn gene cluster from Streptomyces griseochromogenes established the biosynthesis of the TTN polyketide backbone, its dialkylmaleic anhydride moiety, the coupling of the two moieties to form the nascent intermediate TTN F-1, and the tailoring steps converting TTN F-1 to TTN. Here, we report biochemical and structural characterization of TtnD, a prenylated FMN (prFMN)-dependent decarboxylase belonging to the UbiD family that catalyzes the penultimate step of TTN biosynthesis. TtnD catalyzes decarboxylation of TTN D-1 to TTN I-1, utilizing prFMN as a cofactor generated by the TtnC flavin prenyltransferase; both TtnD and TtnC are encoded within the ttn biosynthetic gene cluster. TtnD exhibits substrate promiscuity but accepts only TTN D-1 congeners that feature an alpha,beta-unsaturated acid, supporting the [3+2] cycloaddition mechanism during catalysis that requires the double bond of an alpha,beta-unsaturated acid substrate. TtnD shares a similar overall structure with other members of the UbiD family but forms a homotetramer in solution. Each protomer is composed of three domains with the active site located between the middle and C-terminal domains; R169-E272-E277, constituting the catalytic triad, and E228, involved in Mn(II)-mediated binding of prFMN, were confirmed by site-directed mutagenesis. TtnD represents the first example of a prFMN-dependent decarboxylase involved in polyketide biosynthesis, expanding the substrate scope of the UbiD family of decarboxylases beyond simple aromatic and cinnamic acids. TtnD and its homologues are widespread in nature and could be exploited as biocatalysts for organic synthesis. Biochemical and Structural Characterization of TtnD, a Prenylated FMN-Dependent Decarboxylase from the Tautomycetin Biosynthetic Pathway.,Annaval T, Han L, Rudolf JD, Xie G, Yang D, Chang CY, Ma M, Crnovcic I, Miller MD, Soman J, Xu W, Phillips GN Jr, Shen B ACS Chem Biol. 2018 Sep 21;13(9):2728-2738. doi: 10.1021/acschembio.8b00673. Epub, 2018 Sep 10. PMID:30152678 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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