2JVU

Solution Structure of Dispersin from Enteroaggregative Escherichia coli

2JVU の概要

• エントリーDOI: 10.2210/pdb2jvu/pdb
• 分子名称: DISPERSIN (1 entity in total)
• 機能のキーワード: beta sandwich, unknown function
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11324.38

構造登録者

Velarde, J.J.,Varney, K.M.,Farfan, K.,Dudley, D.,Inman, J.G.,Fletcher, J.,Weber, D.J.,Nataro, J.P. (登録日: 2007-09-25, 公開日: 2008-02-12, 最終更新日: 2024-11-27)

主引用文献

Velarde, J.J.,Varney, K.M.,Inman, K.G.,Farfan, M.,Dudley, E.,Fletcher, J.,Weber, D.J.,Nataro, J.P.
Solution structure of the novel dispersin protein of enteroaggregative Escherichia coli.
Mol.Microbiol., 66:1123-1135, 2007

PubMed Abstract: Enteroaggregative Escherichia coli (EAEC), increasingly recognized as an important cause of infant and travelers' diarrhoea, exhibits an aggregative, stacked-brick pattern of adherence to epithelial cells. Adherence is mediated by aggregative adherence fimbriae (AAFs), which are encoded on the pAA virulence plasmid. We recently described a highly prevalent pAA plasmid-borne gene, aap, which encodes a protein (nicknamed dispersin) that is secreted to the bacterial cell surface. Dispersin-null mutants display a unique hyper-aggregating phenotype, accompanied by collapse of AAF pili onto the bacterial cell surface. To study the mechanism of this effect, we solved the structure of dispersin from EAEC strain 042 using solution NMR, revealing a stable beta-sandwich with a conserved net positive surface charge of +3 to +4 among 23 dispersin alleles. Experimental data suggest that dispersin binds non-covalently to lipopolysaccharide on the surface of the bacterium. We also show that the AAF organelles contribute positive charge to the bacterial surface, suggesting that dispersin's role in fimbrial function is to overcome electrostatic attraction between AAF and the bacterial surface.

PubMed: 17986189
DOI: 10.1111/j.1365-2958.2007.05985.x

実験手法

SOLUTION NMR