1J8S
PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM
Summary for 1J8S
Entry DOI | 10.2210/pdb1j8s/pdb |
Descriptor | PYELONEPHRITIC ADHESIN (2 entities in total) |
Functional Keywords | papg adhesin, receptor, structural protein |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 22768.22 |
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 citation | Dodson, 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: 11440716DOI: 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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