4Z3G

Crystal structure of the lectin domain of PapG from E. coli BI47 in complex with 4-methoxyphenyl beta-D-galabiose in space group P212121

Summary for 4Z3G

• Entry DOI: 10.2210/pdb4z3g/pdb
• Descriptor: PapG, lectin domain, alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (5 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: 2
• Total formula weight: 46834.66

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: 2024-10-23)

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

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: 28076665
DOI: 10.1002/cbic.201600615

Experimental method

X-RAY DIFFRACTION (1.45 Å)