9e4r
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Escherichia coli encapsulin-associated DyP peroxidase== | |
| + | <StructureSection load='9e4r' size='340' side='right'caption='[[9e4r]], [[Resolution|resolution]] 3.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9e4r]] is a 1 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=9E4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9E4R 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]] 3.31Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=9e4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9e4r OCA], [https://pdbe.org/9e4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9e4r RCSB], [https://www.ebi.ac.uk/pdbsum/9e4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9e4r ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A5C9AJY8_ECOLX A0A5C9AJY8_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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 9e4r" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli KTE40]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andreas MP]] | ||
| + | [[Category: Giessen TW]] | ||
| + | [[Category: Ubilla NC]] | ||
Current revision
Escherichia coli encapsulin-associated DyP peroxidase
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