2M8F

Structure of lasso peptide astexin3

2M8F の概要

• エントリーDOI: 10.2210/pdb2m8f/pdb
• NMR情報: BMRB: 19250
• 分子名称: astexin3 (1 entity in total)
• 機能のキーワード: sidechain-to-backbone link, unknown function
• 由来する生物種: Asticcacaulis excentricus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2542.76

構造登録者

Maksimov, M.O.,Link, A. (登録日: 2013-05-18, 公開日: 2013-07-31, 最終更新日: 2024-11-27)

主引用文献

Maksimov, M.O.,Link, A.J.
Discovery and characterization of an isopeptidase that linearizes lasso peptides.
J.Am.Chem.Soc., 135:12038-12047, 2013

PubMed Abstract: Lasso peptides are a class of ribosomally derived natural products with diverse bioactivities. The characteristic threaded lasso structure in these peptides derives from an isopeptide bond attaching the N-terminus of the peptide to an acidic side chain. Here we describe the heterologous expression of a lasso peptide gene cluster encoding two lasso peptides, astexin-2 and astexin-3, and solve the solution structure of astexin-3. This cluster also encodes an enzyme annotated as a protease. We show that this enzyme, AtxE2, is a lasso peptide isopeptidase that specifically hydrolyzes astexins-2 and -3, converting them to linear peptides. Astexin-3 is highly thermostable and resists unthreading after extensive heat treatment. In contrast, astexin-2 unthreads upon heat treatment. AtxE2 has no activity toward unthreaded astexin-2, demonstrating that this isopeptidase must recognize a knotted structure in order to function. We also use this isopeptidase as a tool to study evolutionary relationships between lasso peptide gene clusters.

PubMed: 23862624
DOI: 10.1021/ja4054256

実験手法

SOLUTION NMR