9mne
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of enteropathogenic Escherichia coli EspC== | |
| + | <StructureSection load='9mne' size='340' side='right'caption='[[9mne]], [[Resolution|resolution]] 2.94Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[9mne]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O127:H6_str._E2348/69 Escherichia coli O127:H6 str. E2348/69]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9MNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9MNE FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.94Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=P6G:HEXAETHYLENE+GLYCOL'>P6G</scene>, <scene name='pdbligand=PE8:3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL'>PE8</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=9mne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9mne OCA], [https://pdbe.org/9mne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9mne RCSB], [https://www.ebi.ac.uk/pdbsum/9mne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9mne ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ESPC_ECO27 ESPC_ECO27] Serine protease with enterotoxic and cytotoxic activities. Cleaves fodrin, but does not cause its redistribution within epithelial cells. The exact role of EspC in EPEC pathogenesis is still unknown.<ref>PMID:15155671</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Enteropathogenic E. coli (EPEC) is a significant cause of diarrhea, leading to high infant mortality rates. A key toxin produced by EPEC is the EspC autotransporter, which is regulated alongside genes from the locus of enterocyte effacement (LEE), which collectively result in the characteristic attaching and effacing lesions on the intestinal epithelium. In this study, we present the crystal structure of the EspC passenger domain (alpha(EspC)) revealing a toxin comprised a serine protease attached to a large beta-helix with additional subdomains. Using various modified EspC expression constructs, alongside type III secretion system-mediated cell internalization assays, we dissect how the alpha(EspC) structural features enable toxin entry into the intestinal epithelium to cause cell cytotoxicity. | ||
| - | + | The crystal structure of the toxin EspC from enteropathogenic Escherichia coli reveals the mechanism that governs host cell entry and cytotoxicity.,Pilapitiya AU, Hor L, Pan J, Wijeyewickrema LC, Pike RN, Leyton DL, Paxman JJ, Heras B Gut Microbes. 2025 Dec;17(1):2483777. doi: 10.1080/19490976.2025.2483777. Epub , 2025 Mar 31. PMID:40164999<ref>PMID:40164999</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 9mne" style="background-color:#fffaf0;"></div> |
| - | [[Category: Paxman | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli O127:H6 str. E2348/69]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Heras B]] | ||
| + | [[Category: Paxman JJ]] | ||
| + | [[Category: Pilapitiya AU]] | ||
Current revision
Crystal structure of enteropathogenic Escherichia coli EspC
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