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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11: XN6P4

]

NCBI PubMed ID: 11440716
Journal NLM ID: 0413066
Publisher: Cambridge, MA: Cell Press
Institutions: Department of Molecular Microbiology, Washington University School of Medicine, Saint Louis, MO 63110, USA

PapG is the adhesin at the tip of the P pilus that mediates attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney. The human specific allele of PapG binds to globoside (GbO4), which consists of the tetrasaccharide GalNAc β 1-3Gal α 1-4Gal β 1-4Glc linked to ceramide. Here, we present the crystal structures of a binary complex of the PapG receptor binding domain bound to GbO4 as well as the unbound form of the adhesin. The biological importance of each of the residues involved in binding was investigated by site-directed mutagenesis. These studies provide a molecular snapshot of a host-pathogen interaction that determines the tropism of uropathogenic E. coli for the human kidney and is critical to the pathogenesis of pyelonephritis.

chemistry, Bacterial, metabolism, microbiology, pathogenicity, molecular, X-ray, Escherichia coli, Female, Molecular Sequence Data, proteins, mutagenesis, protein structure, models, amino acid sequence, Sequence Alignment, kidney, Fimbriae, Protein Binding, Crystallography, Humans, Adhesins, Binding Sites, Escherichia coli Infections, Crystallization, Fimbriae Proteins, Globosides, Protein Conformation, Tertiary, Pyelonephritis, Urothelium

Structure type: oligomer
Aglycon: trimethylsylilethyl (instead of natural Cer)
Trivial name: GbO4
Contained glycoepitopes: IEDB_130648,IEDB_130651,IEDB_136044,IEDB_136095,IEDB_136906,IEDB_137339,IEDB_137472,IEDB_137473,IEDB_1391964,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_190606,IEDB_423106,IEDB_742247,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_18,SB_187,SB_192,SB_195,SB_21,SB_27,SB_3,SB_31,SB_5,SB_6,SB_62,SB_7,SB_88

Methods: MAD
Biological activity: binds to PapG
3D data: available

NCBI Taxonomy refs (TaxIDs): 562
Show glycosyltransferases

There are 64 chemically distinct structures. Please, select:

[1*]O[C@@H]1O[C@H](CO)[C@@H](O[C@@H]2O[C@H](CO)[C@H](O[C@H]3O[C@H](CO)[C@H](O)[C@H](O[C@@H]4O[C@H](CO)[C@H](O)[C@H](O)[C@H]4NC(C)=O)[C@H]3O)[C@H](O)[C@H]2O)[C@H](O)[C@H]1O

SVG MW SMILES 3D mol Ionize

R1 = CER