5WJZ

Cryo-EM structure of B. subtilis flagellar filaments E115G

これはPDB形式変換不可エントリーです。

5WJZ の概要

• エントリーDOI: 10.2210/pdb5wjz/pdb
• EMDBエントリー: 8847 8848 8849 8850 8851 8852 8853 8855 8856
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: bacteria flagella, helical polymers, cryo-em, protein fibril
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 46
• 化学式量合計: 1499104.26

構造登録者

Wang, F.,Burrage, A.M.,Orlova, A.,Kearns, D.B.,Egelman, E.H. (登録日: 2017-07-24, 公開日: 2017-10-25, 最終更新日: 2024-03-13)

主引用文献

Wang, F.,Burrage, A.M.,Postel, S.,Clark, R.E.,Orlova, A.,Sundberg, E.J.,Kearns, D.B.,Egelman, E.H.
A structural model of flagellar filament switching across multiple bacterial species.
Nat Commun, 8:960-960, 2017

PubMed Abstract: The bacterial flagellar filament has long been studied to understand how a polymer composed of a single protein can switch between different supercoiled states with high cooperativity. Here we present near-atomic resolution cryo-EM structures for flagellar filaments from both Gram-positive Bacillus subtilis and Gram-negative Pseudomonas aeruginosa. Seven mutant flagellar filaments in B. subtilis and two in P. aeruginosa capture two different states of the filament. These reliable atomic models of both states reveal conserved molecular interactions in the interior of the filament among B. subtilis, P. aeruginosa and Salmonella enterica. Using the detailed information about the molecular interactions in two filament states, we successfully predict point mutations that shift the equilibrium between those two states. Further, we observe the dimerization of P. aeruginosa outer domains without any perturbation of the conserved interior of the filament. Our results give new insights into how the flagellin sequence has been "tuned" over evolution.Bacterial flagellar filaments are composed almost entirely of a single protein-flagellin-which can switch between different supercoiled states in a highly cooperative manner. Here the authors present near-atomic resolution cryo-EM structures of nine flagellar filaments, and begin to shed light on the molecular basis of filament switching.

PubMed: 29038601
DOI: 10.1038/s41467-017-01075-5

実験手法

ELECTRON MICROSCOPY (5.7 Å)