1j8s
PAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORMPAPG ADHESIN RECEPTOR BINDING DOMAIN-UNBOUND FORM
Structural highlights
FunctionPAPG2_ECOLX Tip adhesin component of type P pili that plays a critical role in kidney infection through targeted interaction with the globoseries glycolipids containing the Gal-alpha(1-4)-Gal disaccharide present on uroepithelial cells (PubMed:11440716, PubMed:31361021). In turn, transcriptionally regulates host gene expression in kidney cells, leading to inflammatory pathway activation and renal tissue damage. Acts thereby as key determinant of invasive uropathogenic E.coli (UPEC), which cause pyelonephritis and urinary-source bacteremia (By similarity).[UniProtKB:A0A0H2VAQ6][1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPapG 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. Structural basis of the interaction of the pyelonephritic E. coli adhesin to its human kidney receptor.,Dodson KW, Pinkner JS, Rose T, Magnusson G, Hultgren SJ, Waksman G Cell. 2001 Jun 15;105(6):733-43. PMID:11440716[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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