3tvq | pdb_00003tvq

Crystal structure of TCM Aro/Cyc complexed with trans-dihidroquercetin

spinqualitylabelsall models 3tvq, resolution 1.67Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tvq is a 1 chain structure with sequence from "actinomyces_glaucescens"_preobrazhenskaya_in_gauze_et_al._1957 "actinomyces glaucescens" preobrazhenskaya in gauze et al. 1957. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: DQH Related: 2rer Gene: tcmN ("Actinomyces glaucescens" Preobrazhenskaya in Gauze et al. 1957) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [TCMN_STRGA] The N-terminal domain enhances the formation of an early, partially cyclized intermediate, while the C-terminal domain catalyzes the 3-O-methylation of one or more later intermediates in the biosynthetic pathway. Catalyzes the methylation of tetracenomycin D3 (Tcm D3) to yield Tcm B3. Catalyzes as well the following side reactions: methylation of 8-O-methyl-Tcm D3 to yield Tcm E; and of 9-carboxymethyl-Tcm B3 to yield Tcm A2. Publication Abstract from PubMed Aromatic polyketides are biologically active natural products. Many important pharmaceuticals are derived from aromatic polyketides. Especially important in aromatic polyketide biosynthesis is the regiospecific cyclization of a linear, preassembled polyketide chain catalyzed by aromatase/cyclase (ARO/CYC), which serves as a key control point in aromatic ring formation. How different ARO/CYCs promote different cyclization patterns is not well understood. The whiE locus of Streptomyces coelicolor A3(2) is responsible for the biosynthesis of an aromatic polyketide precursor to the gray spore pigment. The WhiE ARO/CYC catalyzes the regiospecific C9-C14 and C7-C16 cyclization and aromatization of a 24-carbon polyketide chain. WhiE ARO/CYC shares a high degree of similarity to another nonreducing PKS ARO/CYC, TcmN ARO/CYC. This paper presents the apo crystal structure of WhiE ARO/CYC, and cocrystal structures of WhiE and TcmN ARO/CYCs bound with polycyclic aromatic compounds that mimic the respective ARO/CYC products. Site-directed mutagenesis coupled with in vitro PKS reconstitution assays was used to characterize the interior pocket residues of WhiE ARO/CYC. The results confirmed that the interior pocket of ARO/CYCs is a critical determinant of polyketide cyclization specificity. A unified ARO/CYC-mediated cyclization mechanism is proposed on the basis of these structural and functional results. Insight into the Molecular Basis of Aromatic Polyketide Cyclization: Crystal Structure and in Vitro Characterization of WhiE-ORFVI.,Lee MY, Ames BD, Tsai SC Biochemistry. 2012 Mar 30. PMID:22432862 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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