6T17

Cryo-EM structure of the wild-type flagellar filament of the Firmicute Kurthia

これはPDB形式変換不可エントリーです。

6T17 の概要

• エントリーDOI: 10.2210/pdb6t17/pdb
• EMDBエントリー: 10362
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: gram-positive bacteria flagella, helical, wild-type, protein fibril
• 由来する生物種: Kurthia sp. 11kri321
• タンパク質・核酸の鎖数: 44
• 化学式量合計: 1299322.42

構造登録者

Blum, T.B.,Abrahams, J.P. (登録日: 2019-10-03, 公開日: 2019-10-30, 最終更新日: 2024-05-22)

主引用文献

Blum, T.B.,Filippidou, S.,Fatton, M.,Junier, P.,Abrahams, J.P.
The wild-type flagellar filament of the Firmicute Kurthia at 2.8 angstrom resolution in vivo.
Sci Rep, 9:14948-14948, 2019

PubMed Abstract: Bacteria swim and swarm by rotating the micrometers long, helical filaments of their flagella. They change direction by reversing their flagellar rotation, which switches the handedness of the filament's supercoil. So far, all studied functional filaments are composed of a mixture of L- and R-state flagellin monomers. Here we show in a study of the wild type Firmicute Kurthia sp., that curved, functional filaments can adopt a conformation in vivo that is closely related to a uniform, all-L-state. This sheds additional light on transitions of the flagellar supercoil and uniquely reveals the atomic structure of a wild-type flagellar filament in vivo, including six residues showing clearly densities of O-linked glycosylation.

PubMed: 31628388
DOI: 10.1038/s41598-019-51440-1

実験手法

ELECTRON MICROSCOPY (2.8 Å)