View source for 9e5e


==Escherichia coli DyP peroxidase-loaded encapsulin shell==
<StructureSection load='9e5e' size='340' side='right'caption='[[9e5e]], [[Resolution|resolution]] 2.17&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9e5e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_KTE40 Escherichia coli KTE40]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9E5E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9E5E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.17&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9e5e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9e5e OCA], [https://pdbe.org/9e5e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9e5e RCSB], [https://www.ebi.ac.uk/pdbsum/9e5e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9e5e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A3L1NQK1_ECOLX A0A3L1NQK1_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Structural and biochemical characterization of a widespread enterobacterial peroxidase encapsulin.,Ubilla-Rodriguez NC, Andreas MP, Giessen TW bioRxiv [Preprint]. 2024 Dec 3:2024.11.27.625667. doi: 10.1101/2024.11.27.625667. PMID:39651212<ref>PMID:39651212</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9e5e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli KTE40]]
[[Category: Large Structures]]
[[Category: Andreas MP]]
[[Category: Giessen TW]]
[[Category: Ubilla NC]]