View source for 4xoc


==Crystal structure of the FimH lectin domain from E.coli F18 in complex with heptyl alpha-D-mannopyrannoside==
<StructureSection load='4xoc' size='340' side='right'caption='[[4xoc]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4xoc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_536 Escherichia coli 536]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOC 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]] 1.42&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</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=4xoc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xoc OCA], [https://pdbe.org/4xoc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xoc RCSB], [https://www.ebi.ac.uk/pdbsum/4xoc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xoc ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Ligand-receptor interactions that are reinforced by mechanical stress, so-called catch-bonds, play a major role in cell-cell adhesion. They critically contribute to widespread urinary tract infections by pathogenic Escherichia coli strains. These pathogens attach to host epithelia via the adhesin FimH, a two-domain protein at the tip of type I pili recognizing terminal mannoses on epithelial glycoproteins. Here we establish peptide-complemented FimH as a model system for fimbrial FimH function. We reveal a three-state mechanism of FimH catch-bond formation based on crystal structures of all states, kinetic analysis of ligand interaction and molecular dynamics simulations. In the absence of tensile force, the FimH pilin domain allosterically accelerates spontaneous ligand dissociation from the FimH lectin domain by 100,000-fold, resulting in weak affinity. Separation of the FimH domains under stress abolishes allosteric interplay and increases the affinity of the lectin domain. Cell tracking demonstrates that rapid ligand dissociation from FimH supports motility of piliated E. coli on mannosylated surfaces in the absence of shear force.

Catch-bond mechanism of the bacterial adhesin FimH.,Sauer MM, Jakob RP, Eras J, Baday S, Eris D, Navarra G, Berneche S, Ernst B, Maier T, Glockshuber R Nat Commun. 2016 Mar 7;7:10738. doi: 10.1038/ncomms10738. PMID:26948702<ref>PMID:26948702</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4xoc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli 536]]
[[Category: Large Structures]]
[[Category: Ernst B]]
[[Category: Glockshuber R]]
[[Category: Jakob RP]]
[[Category: Maier T]]
[[Category: Navarra G]]
[[Category: Sauer MM]]