8T1T

Structure of the alpha-N-methyltransferase (SonM) and RiPP precursor (SonA with QSY deletion) heteromeric complex (bound to SAM)

8T1T の概要

• エントリーDOI: 10.2210/pdb8t1t/pdb
• 関連するPDBエントリー: 7LTC 7LTE 8T1S
• 分子名称: Alpha-N-methyltransferase (SonM), RiPP precursor (SonA), S-ADENOSYLMETHIONINE, ... (5 entities in total)
• 機能のキーワード: alpha-n-methyltransferase, borosin, natural products, transferase
• 由来する生物種: Shewanella oneidensis; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75807.53

構造登録者

Crone, K.K.,Jomori, T.,Miller, F.S.,Gralnick, J.,Elias, M.,Freeman, M.F. (登録日: 2023-06-03, 公開日: 2023-11-22)

主引用文献

Crone, K.K.,Jomori, T.,Miller, F.S.,Gralnick, J.A.,Elias, M.H.,Freeman, M.F.
RiPP enzyme heterocomplex structure-guided discovery of a bacterial borosin alpha- N -methylated peptide natural product.
Rsc Chem Biol, 4:804-816, 2023

PubMed Abstract: Amide peptide backbone methylation is a characteristic post-translational modification found in a family of ribosomally synthesized and post-translationally modified peptide natural products (RiPPs) called borosins. Previously, we bioinformatically identified >1500 putative borosin pathways in bacteria; however, none of the pathways were associated with a known secondary metabolite. Through in-depth characterization of a borosin pathway in MR-1, we have now identified a bacterially derived borosin natural product named Shewanellamide A. Borosin identification was facilitated by the creation and analysis of a series of precursor variants and crystallographic interrogation of variant precursor and methyltransferase complexes. Along with assaying two proteases from , probable boundaries for proteolytic maturation of the metabolite were projected and confirmed comparison of knockout and overexpression strains. All in all, the natural product was found to be a 16-mer linear peptide featuring two backbone methylations, establishing Shewanellamide A as one of the few borosin metabolites yet identified, and the first from bacteria.

PubMed: 37799586
DOI: 10.1039/d3cb00093a

実験手法

X-RAY DIFFRACTION (1.55 Å)