View source for 8eht


==Cryo-EM reconstruction of the CS20 bacterial adhesion pili==
<StructureSection load='8eht' size='340' side='right'caption='[[8eht]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8eht]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8EHT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8EHT 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]] 3.4&#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=8eht FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8eht OCA], [https://pdbe.org/8eht PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8eht RCSB], [https://www.ebi.ac.uk/pdbsum/8eht PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8eht ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8VL73_ECOLX Q8VL73_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis underpinning the biophysical properties of pili originating from enterotoxigenic (ETEC) and uropathogenic bacteria. Using cryo-electron microscopy we solved the structures of three vaccine target pili from ETEC bacteria, CFA/I, CS17, and CS20. Pairing these and previous pilus structures with force spectroscopy and steered molecular dynamics simulations, we find a strong correlation between subunit-subunit interaction energies and the force required for pilus unwinding, irrespective of genetic similarity. Pili integrate three structural solutions for stabilizing their assemblies: layer-to-layer interactions, N-terminal interactions to distant subunits, and extended loop interactions from adjacent subunits. Tuning of these structural solutions alters the biophysical properties of pili and promotes the superelastic behavior that is essential for sustained bacterial attachment.

Three structural solutions for bacterial adhesion pilus stability and superelasticity.,Doran MH, Baker JL, Dahlberg T, Andersson M, Bullitt E Structure. 2023 May 4;31(5):529-540.e7. doi: 10.1016/j.str.2023.03.005. Epub 2023 , Mar 30. PMID:37001523<ref>PMID:37001523</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8eht" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bullitt E]]
[[Category: Doran MH]]