6MJF

Catalytic Domain of dbOphMA

6MJF の概要

• エントリーDOI: 10.2210/pdb6mjf/pdb
• 分子名称: dbOphM, S-ADENOSYL-L-HOMOCYSTEINE (3 entities in total)
• 機能のキーワード: methyltransferase, borosin, biosynthetic protein
• 由来する生物種: Dendrothele bispora CBS 962.96
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 258750.14

構造登録者

Ongpipatanakul, C.,Nair, S.K. (登録日: 2018-09-20, 公開日: 2018-10-03, 最終更新日: 2024-03-13)

主引用文献

Ongpipattanakul, C.,Nair, S.K.
Molecular Basis for Autocatalytic Backbone N-Methylation in RiPP Natural Product Biosynthesis.
ACS Chem. Biol., 13:2989-2999, 2018

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: 30204409
DOI: 10.1021/acschembio.8b00668

実験手法

X-RAY DIFFRACTION (2.198 Å)