9E5E

Escherichia coli DyP peroxidase-loaded encapsulin shell

9E5E の概要

• エントリーDOI: 10.2210/pdb9e5e/pdb
• EMDBエントリー: 47525
• 分子名称: Bacteriocin, DyP peroxidase (2 entities in total)
• 機能のキーワード: dye-decolorizing peroxidase, peroxidase, dyp, encapsulin, virus like particle
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67377.67

構造登録者

Andreas, M.P.,Ubilla, N.C.,Giessen, T.W. (登録日: 2024-10-28, 公開日: 2025-03-19)

主引用文献

Ubilla-Rodriguez, N.C.,Andreas, M.P.,Giessen, T.W.
Structural and biochemical characterization of a widespread enterobacterial peroxidase encapsulin.
Biorxiv, 2024

PubMed Abstract: Encapsulins are self-assembling protein compartments found in prokaryotes and specifically encapsulate dedicated cargo enzymes. The most abundant encapsulin cargo class are Dye-decolorizing Peroxidases (DyPs). It has been previously suggested that DyP encapsulins are involved in oxidative stress resistance and bacterial pathogenicity due to DyPs' inherent ability to reduce and detoxify hydrogen peroxide while oxidizing a broad range of organic co-substrates. Here, we report the structural and biochemical analysis of a DyP encapsulin widely found across enterobacteria. Using bioinformatic approaches, we show that this DyP encapsulin is encoded by a conserved transposon-associated operon, enriched in enterobacterial pathogens. Through low pH and peroxide exposure experiments, we highlight the stability of this DyP encapsulin under harsh conditions and show that DyP catalytic activity is highest at low pH. We determine the structure of the DyP-loaded shell and free DyP via cryo-electron microscopy, revealing the structural basis for DyP cargo loading and peroxide preference. Our work lays the foundation to further explore the substrate range and physiological functions of enterobacterial DyP encapsulins.

PubMed: 39651212
DOI: 10.1101/2024.11.27.625667

実験手法

ELECTRON MICROSCOPY (2.17 Å)