7ZL4

Cryo-EM structure of archaic chaperone-usher Csu pilus of Acinetobacter baumannii

7ZL4 の概要

• エントリーDOI: 10.2210/pdb7zl4/pdb
• 関連するPDBエントリー: 6FM5
• EMDBエントリー: 14777
• 分子名称: CsuA/B (1 entity in total)
• 機能のキーワード: chaperone-usher pathway, bacterial adhesion, biofilm formation, acinetobacter baumannii, csu pili, cell adhesion
• 由来する生物種: Acinetobacter baumannii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64278.57

構造登録者

Pakharukova, N.,Malmi, H.,Tuittila, M.,Paavilainen, S.,Ghosal, D.,Chang, Y.W.,Jensen, G.J.,Zavialov, A.V. (登録日: 2022-04-13, 公開日: 2022-08-03, 最終更新日: 2024-10-23)

主引用文献

Pakharukova, N.,Malmi, H.,Tuittila, M.,Dahlberg, T.,Ghosal, D.,Chang, Y.W.,Myint, S.L.,Paavilainen, S.,Knight, S.D.,Lamminmaki, U.,Uhlin, B.E.,Andersson, M.,Jensen, G.,Zavialov, A.V.
Archaic chaperone-usher pili self-secrete into superelastic zigzag springs.
Nature, 609:335-340, 2022

PubMed Abstract: Adhesive pili assembled through the chaperone-usher pathway are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria. Archaic chaperone-usher pathway pili, the most diverse and widespread chaperone-usher pathway adhesins, are promising vaccine and drug targets owing to their prevalence in the most troublesome multidrug-resistant pathogens. However, their architecture and assembly-secretion process remain unknown. Here, we present the cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii-a notorious multidrug-resistant nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into an ultrathin zigzag architecture secured by an elegant clinch mechanism. The molecular clinch provides the pilus with high mechanical stability as well as superelasticity, a property observed for the first time, to our knowledge, in biomolecules, while enabling a more economical and faster pilus production. Furthermore, we demonstrate that clinch formation at the cell surface drives pilus secretion through the outer membrane. These findings suggest that clinch-formation inhibitors might represent a new strategy to fight multidrug-resistant bacterial infections.

PubMed: 35853476
DOI: 10.1038/s41586-022-05095-0

実験手法

ELECTRON MICROSCOPY (3.45 Å)