4xoe

Crystal structure of a FimH*DsG complex from E.coli F18 with bound heptyl alpha-D-mannopyrannoside

spinqualitylabelsall models 4xoe, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xoe is a 2 chain structure with sequence from Escherichia coli 536. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CAC, KGM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A140UH97_ECOL5 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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