6MJG
Structure of dbOphMA in Complex with SAH and Methylated Peptide
Summary for 6MJG
| Entry DOI | 10.2210/pdb6mjg/pdb |
| Descriptor | fusion protein of dbOphMA and methylated peptide, S-ADENOSYL-L-HOMOCYSTEINE, ZINC ION, ... (4 entities in total) |
| Functional Keywords | methyltransferase, borosin, biosynthetic protein |
| Biological source | Dendrothele bispora CBS 962.96 More |
| Total number of polymer chains | 1 |
| Total formula weight | 46672.33 |
| Authors | Ongpipattanakul, C.,Nair, S.K. (deposition date: 2018-09-20, release date: 2018-10-03, Last modification date: 2024-11-13) |
| Primary citation | Ongpipattanakul, C.,Nair, S.K. Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis. ACS Chem. Biol., 13:2989-2999, 2018 Cited by PubMed Abstract: 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 α-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. PubMed: 30204409DOI: 10.1021/acschembio.8b00668 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.123 Å) |
Structure validation
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