7LHH

Cryo-EM structure of E. coli P pilus tip assembly intermediate PapC-PapD-PapK-PapG in the second conformation

7LHH の概要

• エントリーDOI: 10.2210/pdb7lhh/pdb
• EMDBエントリー: 23339 23340 23341
• 分子名称: P fimbrial usher protein PapC, Chaperone protein PapD, Fimbrial adapter PapK, ... (4 entities in total)
• 機能のキーワード: cryo-em, uropathogenic escherichia coli, chaperone-usher, p pilus, chaperone
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 169852.25

構造登録者

Du, M.,Yuan, Z.,Werneburg, G.,Henderson, N.,Chauhan, H.,Kovach, A.,Zhao, G.,Johl, J.,Li, H.,Thanassi, D. (登録日: 2021-01-23, 公開日: 2021-08-11, 最終更新日: 2024-05-29)

主引用文献

Du, M.,Yuan, Z.,Werneburg, G.T.,Henderson, N.S.,Chauhan, H.,Kovach, A.,Zhao, G.,Johl, J.,Li, H.,Thanassi, D.G.
Processive dynamics of the usher assembly platform during uropathogenic Escherichia coli P pilus biogenesis.
Nat Commun, 12:5207-5207, 2021

PubMed Abstract: Uropathogenic Escherichia coli assemble surface structures termed pili or fimbriae to initiate infection of the urinary tract. P pili facilitate bacterial colonization of the kidney and pyelonephritis. P pili are assembled through the conserved chaperone-usher pathway. Much of the structural and functional understanding of the chaperone-usher pathway has been gained through investigations of type 1 pili, which promote binding to the bladder and cystitis. In contrast, the structural basis for P pilus biogenesis at the usher has remained elusive. This is in part due to the flexible and variable-length P pilus tip fiber, creating structural heterogeneity, and difficulties isolating stable P pilus assembly intermediates. Here, we circumvent these hindrances and determine cryo-electron microscopy structures of the activated PapC usher in the process of secreting two- and three-subunit P pilus assembly intermediates, revealing processive steps in P pilus biogenesis and capturing new conformational dynamics of the usher assembly machine.

PubMed: 34471127
DOI: 10.1038/s41467-021-25522-6

実験手法

ELECTRON MICROSCOPY (7.2 Å)