5thy | pdb_00005thy

Crystal structure of SeMet-Substituted CurJ carbon methyltransferase

spinqualitylabelsall models 5thy, resolution 2.09Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5thy is a 2 chain structure with sequence from Lyngbya majuscula 3l. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GDS, SAH NonStd Res: MSE Related: 5thz Gene: LYNGBM3L_74460 (Lyngbya majuscula 3L) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Polyketide metabolites produced by modular type I polyketide synthases (PKS) acquire their chemical diversity through the variety of catalytic domains within modules of the pathway. Methyltransferases are among the least characterized of the catalytic domains common to PKS systems. We determined the domain boundaries and characterized the activity of a PKS C-methyltransferase (C-MT) from the curacin A biosynthetic pathway. The C-MT catalyzes S-adenosylmethionine-dependent methyl transfer to the alpha-position of beta-ketoacyl substrates linked to acyl carrier protein (ACP) or a small-molecule analog, but does not act on beta-hydroxyacyl substrates or malonyl-ACP. Key catalytic residues conserved in both bacterial and fungal PKS C-MTs were identified in a 2-A crystal structure and validated biochemically. Analysis of the structure and the sequences bordering the C-MT provides insight into the positioning of this domain within complete PKS modules. Domain Organization and Active Site Architecture of a Polyketide Synthase C-methyltransferase.,Skiba MA, Sikkema AP, Fiers WD, Gerwick WH, Sherman DH, Aldrich CC, Smith JL ACS Chem Biol. 2016 Oct 10. PMID:27723289 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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