4MEE

Crystal structure of the transport unit of the autotransporter AIDA-I from Escherichia coli

4MEE の概要

• エントリーDOI: 10.2210/pdb4mee/pdb
• 分子名称: Diffuse adherence adhesin (1 entity in total)
• 機能のキーワード: beta barrel, outer membrane protein, autotransporter, protein binding
• 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: 50952.49

構造登録者

Gawarzewski, I.,Tschapek, B.,Hoeppner, A.,Smits, S.H.,Jose, J.,Schmitt, L. (登録日: 2013-08-26, 公開日: 2014-06-04, 最終更新日: 2024-02-28)

主引用文献

Gawarzewski, I.,DiMaio, F.,Winterer, E.,Tschapek, B.,Smits, S.H.,Jose, J.,Schmitt, L.
Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli.
J.Struct.Biol., 187:20-29, 2014

PubMed Abstract: Several serious gastrointestinal diseases, which are widespread all over the world, are caused by enteropathogenic Escherichia coli. The monomeric autotransporter AIDA-I (adhesin involved in diffuse adherence) represents an important virulence factor of these strains and is involved in adhesion, biofilm formation, aggregation and invasion into host cells. Here, we present the crystal structure of the transport unit of AIDA-I at 3.0Å resolution, which forms a 12-stranded β-barrel harboring the linker domain in its pore. Mutagenesis studies of the C-terminal amino acid demonstrated the great impact of this terminal residue on membrane integration of AIDA-I and passenger translocation.

PubMed: 24841284
DOI: 10.1016/j.jsb.2014.05.003

実験手法

X-RAY DIFFRACTION (3 Å)