6XXD

CryoEM structure of the type IV pilin PilA4 from Thermus thermophilus

6XXD の概要

• エントリーDOI: 10.2210/pdb6xxd/pdb
• EMDBエントリー: 10647
• 分子名称: PilA (1 entity in total)
• 機能のキーワード: type iv pilin glycosylation twitching motility, cell adhesion
• 由来する生物種: Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 212017.97

構造登録者

Neuhaus, A.,Gold, V.A.M. (登録日: 2020-01-27, 公開日: 2020-03-11, 最終更新日: 2024-11-20)

主引用文献

Neuhaus, A.,Selvaraj, M.,Salzer, R.,Langer, J.D.,Kruse, K.,Kirchner, L.,Sanders, K.,Daum, B.,Averhoff, B.,Gold, V.A.M.
Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.
Nat Commun, 11:2231-2231, 2020

PubMed Abstract: Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.

PubMed: 32376942
DOI: 10.1038/s41467-020-15650-w

実験手法

ELECTRON MICROSCOPY (3.22 Å)