2IXQ

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

2IXQ の概要

• エントリーDOI: 10.2210/pdb2ixq/pdb
• 関連するPDBエントリー: 1RXL 1USZ 1UT2
• 分子名称: Protein AfaD, Afimbrial adhesin AFA-III (2 entities in total)
• 機能のキーワード: ig-like domain, afimbrial sheath, structural protein, donor strand complemented, cell adhesion, daf, afae, upec, daec, fimbria
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 30767.92

構造登録者

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. (登録日: 2006-07-10, 公開日: 2006-09-20, 最終更新日: 2024-10-09)

主引用文献

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

実験手法

SOLUTION NMR