4Z3H

Crystal structure of the lectin domain of PapG from E. coli BI47 in complex with 4-methoxyphenyl beta-D-galabiose in space group P21

4Z3H の概要

• エントリーDOI: 10.2210/pdb4z3h/pdb
• 分子名称: PapG, lectin domain, alpha-D-galactopyranose-(1-4)-beta-D-galactopyranose, 4-methoxyphenol, ... (4 entities in total)
• 機能のキーワード: upec, urinary tract infection, fimbrial adhesin, adhesin, type i pili, papg, carbohydrate binding, sugar binding protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23222.09

構造登録者

Jakob, R.P.,Navarra, G.,Zihlmann, P.,Stangier, K.,Preston, R.C.,Rabbani, S.,Maier, T.,Ernst, B. (登録日: 2015-03-31, 公開日: 2016-04-13, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)