2ixq
From Proteopedia
THE SOLUTION STRUCTURE OF THE INVASIVE TIP COMPLEX FROM AFA-DR FIBRILS
Overview
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.
About this Structure
2IXQ is a Protein complex structure. Full crystallographic information is available from OCA.
Reference
The solution structure of the invasive tip complex from Afa/Dr fibrils., Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S, Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519 Page seeded by OCA on Sun May 4 08:02:50 2008
Categories: Protein complex | Altroff, H. | Anderson, K L. | Bouguenec, C Le. | Cota, E. | Guignot, J. | Jones, C. | Mardon, H. | Matthews, S. | Merle, L Du. | Servin, A. | Simpson, P. | Afae | Afimbrial sheath | Cell adhesion | Daec | Daf | Donor strand complemented | Fimbria | Ig-like domain | Structural protein | Upec
