8EHT

Cryo-EM reconstruction of the CS20 bacterial adhesion pili

8EHT の概要

• エントリーDOI: 10.2210/pdb8eht/pdb
• EMDBエントリー: 28152
• 分子名称: CS20 fimbria major subunit protein (1 entity in total)
• 機能のキーワード: enterotoxigenic, adhesion pili, superelastic, cell adhesion
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 122046.39

構造登録者

Doran, M.H.,Bullitt, E. (登録日: 2022-09-14, 公開日: 2023-03-22, 最終更新日: 2024-10-23)

主引用文献

Doran, M.H.,Baker, J.L.,Dahlberg, T.,Andersson, M.,Bullitt, E.
Three structural solutions for bacterial adhesion pilus stability and superelasticity.
Structure, 31:529-540.e7, 2023

PubMed Abstract: Bacterial adhesion pili are key virulence factors that mediate host-pathogen interactions in diverse epithelial environments. Deploying a multimodal approach, we probed the structural basis underpinning the biophysical properties of pili originating from enterotoxigenic (ETEC) and uropathogenic bacteria. Using cryo-electron microscopy we solved the structures of three vaccine target pili from ETEC bacteria, CFA/I, CS17, and CS20. Pairing these and previous pilus structures with force spectroscopy and steered molecular dynamics simulations, we find a strong correlation between subunit-subunit interaction energies and the force required for pilus unwinding, irrespective of genetic similarity. Pili integrate three structural solutions for stabilizing their assemblies: layer-to-layer interactions, N-terminal interactions to distant subunits, and extended loop interactions from adjacent subunits. Tuning of these structural solutions alters the biophysical properties of pili and promotes the superelastic behavior that is essential for sustained bacterial attachment.

PubMed: 37001523
DOI: 10.1016/j.str.2023.03.005

実験手法

ELECTRON MICROSCOPY (3.4 Å)