6mjg | pdb_00006mjg

Structure of dbOphMA in Complex with SAH and Methylated Peptide

spinqualitylabelsall models 6mjg, resolution 2.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6mjg is a 1 chain structure with sequence from Dendrothele bispora CBS 962.96. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.123Å Ligands: IML, MVA, SAH, SAR, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DBIMA_DENBC Fusion protein of the methyltransferase dbiM and the dendrothelin core peptide; part of the gene cluster that mediates the biosynthesis of dendrothelin A, a highly methylated cyclic dodecapeptide showing slight nematodicidal activity (PubMed:30204409, PubMed:33574430). Dendrothelin A derives from the C-terminus of the dbiMA protein, and it is the dbiMA protein that methylates its own C-terminus using S-adenosyl methionine (SAM) (PubMed:30204409, PubMed:33574430). The C-terminus is subsequently cleaved off and macrocyclized by the prolyloligopeptidase dbiP to give the final product (PubMed:30204409, PubMed:33574430). Publication Abstract from PubMed N-methylation of nucleic acids, proteins, and peptides is a chemical modification with significant impact on biological regulation. Despite the simplicity of the structural change, N-methylation can influence diverse functions including epigenetics, protein complex formation, and microtubule stability. While there are limited examples of N-methylation of the alpha-amino group of bacterial and eukaryotic proteins, there are no examples of catalysts that carry out post-translation methylation of backbone amides in proteins or peptides. Recent studies have identified enzymes that catalyze backbone N-methylation on a peptide substrate, a reaction with little biochemical precedent, in a family of ribosomally synthesized natural products produced in basidiomycetes. Here, we describe the crystal structures of Dendrothele bispora dbOphMA, a methyltransferase that catalyzes multiple N-methylations on the peptide backbone. We further carry out biochemical studies of this catalyst to determine the molecular details that promote this unusual chemical transformation. The structural and biochemical framework described here could facilitate biotechnological applications of catalysts for the rapid production of backbone N-methylated peptides. Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.,Ongpipattanakul C, Nair SK ACS Chem Biol. 2018 Sep 25. doi: 10.1021/acschembio.8b00668. PMID:30204409 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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