7D84

34-fold symmetry Salmonella S ring formed by full-length FliF

7D84 の概要

• エントリーDOI: 10.2210/pdb7d84/pdb
• EMDBエントリー: 30612
• 分子名称: Flagellar M-ring protein (1 entity in total)
• 機能のキーワード: flagellar motor, type iii protein export system, transmembrane protein complex, torque generation, membrane protein
• 由来する生物種: Salmonella enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 2084051.93

構造登録者

Kawamoto, A.,Miyata, T.,Makino, F.,Kinoshita, M.,Minamino, T.,Imada, K.,Kato, T.,Namba, K. (登録日: 2020-10-07, 公開日: 2021-05-19, 最終更新日: 2024-03-27)

主引用文献

Kawamoto, A.,Miyata, T.,Makino, F.,Kinoshita, M.,Minamino, T.,Imada, K.,Kato, T.,Namba, K.
Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries.
Nat Commun, 12:4223-4223, 2021

PubMed Abstract: The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. The C ring attached to the MS ring is involved in torque generation and rotation switch, and a large symmetry mismatch between these two rings has been a long puzzle, especially with respect to their role in motor function. Here, using cryoEM structural analysis of the flagellar basal body and the MS ring formed by full-length FliF from Salmonella enterica, we show that the native MS ring is formed by 34 FliF subunits with no symmetry variation. Symmetry analysis of the C ring shows a variation with a peak at 34-fold, suggesting flexibility in C ring assembly. Finally, our data also indicate that FliF subunits assume two different conformations, contributing differentially to the inner and middle parts of the M ring and thus resulting in 23- and 11-fold subsymmetries in the inner and middle M ring, respectively. The internal core of the M ring, formed by 23 subunits, forms a hole of the right size to accommodate the protein export gate.

PubMed: 34244518
DOI: 10.1038/s41467-021-24507-9

実験手法

ELECTRON MICROSCOPY (3.7 Å)