8bic

O-Methyltransferase Plu4891 in complex with SAH

spinqualitylabelsall models 8bic, resolution 1.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bic is a 2 chain structure with sequence from Photorhabdus laumondii subsp. laumondii TTO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.85Å Ligands: GOL, NA, SAH Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q7MY07_PHOLL Publication Abstract from PubMed Modification of the polyketide anthraquinone AQ-256 in the entomopathogenic Photorhabdus luminescens involves several O-methylations, but the biosynthetic gene cluster antA-I lacks corresponding tailoring enzymes. We here describe the identification of five putative, highly homologous O-methyltransferases encoded in the genome of P. luminescens. Activity assays in vitro and deletion experiments in vivo revealed that three of them account for anthraquinone tailoring by producing three monomethylated and two dimethylated species of AQ-256. X-ray structures of all five enzymes indicate high structural and mechanistic similarity. As confirmed by structure-based mutagenesis, a conserved histidine at the active site likely functions as a general base for substrate deprotonation and subsequent methyl transfer in all enzymes. Eight complex structures with AQ-256 as well as mono- and dimethylated derivatives confirm the substrate specificity patterns found in vitro and visualize how single amino acid differences in the active-site pockets impact substrate orientation and govern site-specific methylation. A set of closely related methyltransferases for site-specific tailoring of anthraquinone pigments.,Huber EM, Kreling L, Heinrich AK, Dunnebacke M, Pothig A, Bode HB, Groll M Structure. 2023 May 4;31(5):573-583.e5. doi: 10.1016/j.str.2023.03.001. Epub 2023 , Mar 23. PMID:36963398 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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