4xob: Difference between revisions
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==Crystal structure of a FimH*DsF complex from E.coli K12 with bound heptyl alpha-D-mannopyrannoside== | ==Crystal structure of a FimH*DsF complex from E.coli K12 with bound heptyl alpha-D-mannopyrannoside== | ||
<StructureSection load='4xob' size='340' side='right' caption='[[4xob]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='4xob' size='340' side='right'caption='[[4xob]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xob]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOB OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4xob]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XOB FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.003Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4xob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xob OCA], [https://pdbe.org/4xob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xob RCSB], [https://www.ebi.ac.uk/pdbsum/4xob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xob ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. | ||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4xob" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Adhesin 3D structures|Adhesin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia coli K-12]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Eras J]] | ||
[[Category: | [[Category: Ernst B]] | ||
[[Category: | [[Category: Glockshuber R]] | ||
[[Category: | [[Category: Jakob RP]] | ||
[[Category: | [[Category: Maier T]] | ||
[[Category: | [[Category: Navarra G]] | ||
Latest revision as of 13:49, 10 January 2024
Crystal structure of a FimH*DsF complex from E.coli K12 with bound heptyl alpha-D-mannopyrannosideCrystal structure of a FimH*DsF complex from E.coli K12 with bound heptyl alpha-D-mannopyrannoside
Structural highlights
FunctionFIMH_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed. Publication Abstract from PubMedLigand-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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