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1J8S

PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM

Summary for 1J8S
Entry DOI10.2210/pdb1j8s/pdb
DescriptorPYELONEPHRITIC ADHESIN (2 entities in total)
Functional Keywordspapg adhesin, receptor, structural protein
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight22768.22
Authors
Dodson, K.W.,Pinkner, J.S.,Rose, T.,Magnusson, G.,Hultgren, S.J.,Waksman, G. (deposition date: 2001-05-22, release date: 2001-06-22, Last modification date: 2024-10-16)
Primary citationDodson, K.W.,Pinkner, J.S.,Rose, T.,Magnusson, G.,Hultgren, S.J.,Waksman, G.
Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor.
Cell(Cambridge,Mass.), 105:733-743, 2001
Cited by
PubMed Abstract: 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 beta 1-3Gal alpha 1-4Gal beta 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.
PubMed: 11440716
DOI: 10.1016/S0092-8674(01)00388-9
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.1 Å)
Structure validation

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