4z3i

Crystal structure of the lectin domain of PapG from E. coli BI47 in spacegroup P21212

spinqualitylabelsall models 4z3i, resolution 1.74Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4z3i is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.739Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A182DW20_ECOLX Publication Abstract from PubMed Uropathogenic E. coli exploit the PapG-II adhesin for infecting host cells of the kidney; moreover, the expression of PapG-II located at the tip of bacterial pili has been correlated with the onset of pyelonephritis in humans, a potentially life-threatening condition. It was envisaged that the blocking of PapG-II, and thus bacterial adhesion, embodies a viable therapeutic alternative to conventional antibiotic treatment. Within our search for potent PapG-II antagonists, we observed an increase in affinity when tetrasaccharide 1, the natural ligand of PapG-II in human kidneys, was elongated to hexasaccharide 2, although the additional Siaalpha(2-3)Gal extension is not in direct contact with the lectin. ITC studies suggest that the increased affinity results from partial desolvation of non-binding regions of the hexasaccharide, and is ultimately connected to the perturbation of outer hydration layers. Our results are in agreement with previous observations and suggest a general mechanism for modulating carbohydrate-protein interactions based on non-binding regions of the ligand. Carbohydrate-Lectin Interactions - An Unexpected Contribution to Affinity.,Navarra G, Zihlmann P, Jakob RP, Stangier K, Preston RC, Rabbani S, Smiesko M, Wagner B, Maier T, Ernst B Chembiochem. 2017 Jan 11. doi: 10.1002/cbic.201600615. PMID:28076665 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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