2FVN
The fibrillar tip complex of the Afa/Dr adhesins from pathogen E. coli displays synergistic binding to 5 1 and v 3 integrins
Summary for 2FVN
| Entry DOI | 10.2210/pdb2fvn/pdb |
| Related | 1RXL |
| NMR Information | BMRB: 5946 |
| Descriptor | Protein afaD (1 entity in total) |
| Functional Keywords | afad, afae, fibrillar, afimbrial, integrin-binding, daec, daf, ceacam, cell adhesion |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 16630.32 |
| Authors | Cota, E.,Simpson, P.,Anderson, K.L.,Matthews, S.J. (deposition date: 2006-01-31, release date: 2007-02-27, Last modification date: 2024-10-23) |
| 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 Cited by 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: 16965519DOI: 10.1111/j.1365-2958.2006.05375.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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