2IXQ

The solution structure of the invasive tip complex from Afa-Dr fibrils

Summary for 2IXQ

• Entry DOI: 10.2210/pdb2ixq/pdb
• Related: 1RXL 1USZ 1UT2
• Descriptor: Protein AfaD, Afimbrial adhesin AFA-III (2 entities in total)
• Functional Keywords: ig-like domain, afimbrial sheath, structural protein, donor strand complemented, cell adhesion, daf, afae, upec, daec, fimbria
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 30767.92

Authors

Cota, E.,Jones, C.,Simpson, P.,Altroff, H.,Anderson, K.L.,du Merle, L.,Guignot, J.,Servin, A.,Le Bouguenec, C.,Mardon, H.,Matthews, S. (deposition date: 2006-07-10, release date: 2006-09-20, Last modification date: 2024-10-09)

Primary citation

Cota, E.,Jones, C.,Simpson, P.,Altroff, H.,Anderson, K.L.,du Merle, L.,Guignot, J.,Servin, A.,Le Bouguenec, C.,Mardon, H.,Matthews, S.
The solution structure of the invasive tip complex from Afa/Dr fibrils.
Mol. Microbiol., 62:356-366, 2006

PubMed Abstract: Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.

PubMed: 16965519
DOI: 10.1111/j.1365-2958.2006.05375.x

Experimental method

SOLUTION NMR