8PSV

2.7 A cryo-EM structure of in vitro assembled type 1 pilus rod

8PSV の概要

• エントリーDOI: 10.2210/pdb8psv/pdb
• EMDBエントリー: 17863
• 分子名称: Type-1 fimbrial protein, A chain (1 entity in total)
• 機能のキーワード: fima, pilus, monomer, subunit, pili, main structural subunit, high resolution, structural protein, cryo-em, helical processing, relion, chaperone-usher pilus
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 108726.44

構造登録者

Hospenthal, M.,Zyla, D.,Glockshuber, R.,Waksman, G. (登録日: 2023-07-13, 公開日: 2024-04-10, 最終更新日: 2024-11-13)

主引用文献

Zyla, D.S.,Wiegand, T.,Bachmann, P.,Zdanowicz, R.,Giese, C.,Meier, B.H.,Waksman, G.,Hospenthal, M.K.,Glockshuber, R.
The assembly platform FimD is required to obtain the most stable quaternary structure of type 1 pili.
Nat Commun, 15:3032-3032, 2024

PubMed Abstract: Type 1 pili are important virulence factors of uropathogenic Escherichia coli that mediate bacterial attachment to epithelial cells in the urinary tract. The pilus rod is comprised of thousands of copies of the main structural subunit FimA and is assembled in vivo by the assembly platform FimD. Although type 1 pilus rods can self-assemble from FimA in vitro, this reaction is slower and produces structures with lower kinetic stability against denaturants compared to in vivo-assembled rods. Our study reveals that FimD-catalysed in vitro-assembled type 1 pilus rods attain a similar stability as pilus rods assembled in vivo. Employing structural, biophysical and biochemical analyses, we show that in vitro assembly reactions lacking FimD produce pilus rods with structural defects, reducing their stability against dissociation. Overall, our results indicate that FimD is not only required for the catalysis of pilus assembly, but also to control the assembly of the most stable quaternary structure.

PubMed: 38589417
DOI: 10.1038/s41467-024-47212-9

実験手法

ELECTRON MICROSCOPY (2.7 Å)