4Z3J
Crystal structure of the lectin domain of PapG from E. coli BI47 in space group P1
Summary for 4Z3J
| Entry DOI | 10.2210/pdb4z3j/pdb |
| Descriptor | PapG, lectin domain (2 entities in total) |
| Functional Keywords | upec, urinary tract infection, fimbrial adhesin, adhesin, type i pili, papg, carbohydrate binding, sugar binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 91022.64 |
| Authors | Jakob, R.P.,Navarra, G.,Zihlmann, P.,Stangier, K.,Preston, R.C.,Rabbani, S.,Maier, T.,Ernst, B. (deposition date: 2015-03-31, release date: 2016-04-13, Last modification date: 2024-11-06) |
| Primary citation | Navarra, G.,Zihlmann, P.,Jakob, R.P.,Stangier, K.,Preston, R.C.,Rabbani, S.,Smiesko, M.,Wagner, B.,Maier, T.,Ernst, B. Carbohydrate-Lectin Interactions: An Unexpected Contribution to Affinity. Chembiochem, 18:539-544, 2017 Cited by PubMed Abstract: Uropathogenic E. coli exploit PapG-II adhesin for infecting host cells of the kidney; the expression of PapG-II at the tip of bacterial pili correlates with the onset of pyelonephritis in humans, a potentially life-threatening condition. It was envisaged that blocking PapG-II (and thus bacterial adhesion) would provide a viable therapeutic alternative to conventional antibiotic treatment. In 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, even though the additional Siaα(2-3)Gal extension is not in direct contact with the lectin. ITC studies suggest that the increased affinity results from partial desolvation of nonbinding regions of the hexasaccharide; this is ultimately responsible for perturbation of the outer hydration layers. Our results are in agreement with previous observations and suggest a general mechanism for modulating carbohydrate-protein interactions based on nonbinding regions of the ligand. PubMed: 28076665DOI: 10.1002/cbic.201600615 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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