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9E5E

Escherichia coli DyP peroxidase-loaded encapsulin shell

Summary for 9E5E
Entry DOI10.2210/pdb9e5e/pdb
EMDB information47525
DescriptorBacteriocin, DyP peroxidase (2 entities in total)
Functional Keywordsdye-decolorizing peroxidase, peroxidase, dyp, encapsulin, virus like particle
Biological sourceEscherichia coli
More
Total number of polymer chains2
Total formula weight67377.67
Authors
Andreas, M.P.,Ubilla, N.C.,Giessen, T.W. (deposition date: 2024-10-28, release date: 2025-03-19)
Primary citationUbilla-Rodriguez, N.C.,Andreas, M.P.,Giessen, T.W.
Structural and biochemical characterization of a widespread enterobacterial peroxidase encapsulin.
Biorxiv, 2024
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.17 Å)
Structure validation

237735

数据于2025-06-18公开中

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