1ZWT

Structure of the globular head domain of the bundlin, BfpA, of the bundle-forming pilus of Enteropathogenic E.coli

1ZWT の概要

• エントリーDOI: 10.2210/pdb1zwt/pdb
• 分子名称: Major structural subunit of bundle-forming pilus (1 entity in total)
• 機能のキーワード: alpha-beta fold, beta-sandwich, one disulfide bond, cell adhesion
• 由来する生物種: Escherichia coli
• 細胞内の位置: Fimbrium: P33553
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16486.09

構造登録者

Ramboarina, S.,Fernandes, P.J.,Daniell, S.,Islam, S.,Frankel, G.,Booy, F.,Donnenberg, M.S.,Matthews, S. (登録日: 2005-06-06, 公開日: 2005-10-04, 最終更新日: 2024-11-13)

主引用文献

Ramboarina, S.,Fernandes, P.J.,Daniell, S.,Islam, S.,Simpson, P.,Frankel, G.,Booy, F.,Donnenberg, M.S.,Matthews, S.
Structure of the Bundle-forming Pilus from Enteropathogenic Escherichia coli
J.Biol.Chem., 280:40252-40260, 2005

PubMed Abstract: Bundle-forming pili (BFP) are essential for the full virulence of enteropathogenic Escherichia coli (EPEC) because they are required for localized adherence to epithelial cells and auto-aggregation. We report the high resolution structure of bundlin, the monomer of BFP, solved by NMR. The structure reveals a new variation in the topology of type IVb pilins with significant differences in the composition and relative orientation of elements of secondary structure. In addition, the structural parameters of native BFP filaments were determined by electron microscopy after negative staining. The solution structure of bundlin was assembled according to these helical parameters to provide a plausible atomic resolution model for the BFP filament. We show that EPEC and Vibriocholerae type IVb pili display distinct differences in their monomer subunits consistent with data showing that bundlin and TcpA cannot complement each other, but assemble into filaments with similar helical organization.

PubMed: 16172128
DOI: 10.1074/jbc.M508099200

実験手法

SOLUTION NMR