7LTR

Structure of the heteromeric complex between the alpha-N-methyltransferase (SonM) and a truncated construct of the RiPP precursor (SonA) (with SAM)

7LTR の概要

• エントリーDOI: 10.2210/pdb7ltr/pdb
• 関連するPDBエントリー: 7LTC 7LTE 7LTF 7LTH
• 分子名称: TP-methylase family protein, LigA domain-containing protein, S-ADENOSYLMETHIONINE, ... (5 entities in total)
• 機能のキーワード: posttranslational modifications; ribosomally synthesized and posttranslationally modified peptides; alpha-n-methyltransferase; borosin; sam, transferase
• 由来する生物種: Shewanella oneidensis; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 148728.95

構造登録者

Miller, F.S.,Crone, K.K.,Jensen, M.R.,Shaw, S.,Harcombe, W.R.,Elias, M.,Freeman, M.F. (登録日: 2021-02-19, 公開日: 2021-09-29, 最終更新日: 2023-10-18)

主引用文献

Miller, F.S.,Crone, K.K.,Jensen, M.R.,Shaw, S.,Harcombe, W.R.,Elias, M.H.,Freeman, M.F.
Conformational rearrangements enable iterative backbone N-methylation in RiPP biosynthesis.
Nat Commun, 12:5355-5355, 2021

PubMed Abstract: Peptide backbone α-N-methylations change the physicochemical properties of amide bonds to provide structural constraints and other favorable characteristics including biological membrane permeability to peptides. Borosin natural product pathways are the only known ribosomally encoded and posttranslationally modified peptides (RiPPs) pathways to incorporate backbone α-N-methylations on translated peptides. Here we report the discovery of type IV borosin natural product pathways (termed 'split borosins'), featuring an iteratively acting α-N-methyltransferase and separate precursor peptide substrate from the metal-respiring bacterium Shewanella oneidensis. A series of enzyme-precursor complexes reveal multiple conformational states for both α-N-methyltransferase and substrate. Along with mutational and kinetic analyses, our results give rare context into potential strategies for iterative maturation of RiPPs.

PubMed: 34504067
DOI: 10.1038/s41467-021-25575-7

実験手法

X-RAY DIFFRACTION (1.75 Å)