6JY0

CryoEM structure of S.typhimurium R-type straight flagellar filament made of FljB (A461V)

6JY0 の概要

• エントリーDOI: 10.2210/pdb6jy0/pdb
• EMDBエントリー: 0980 9896
• 分子名称: Flagellin (1 entity in total)
• 機能のキーワード: fljb, helical reconstruction, salmonella, flagellar motor, protein fibril
• 由来する生物種: Salmonella enterica subsp. enterica serovar Typhimurium
• タンパク質・核酸の鎖数: 22
• 化学式量合計: 1157385.88

構造登録者

Yamaguchi, T.,Toma, S.,Terahara, N.,Miyata, T.,Minamino, T.,Ashikara, M.,Namba, K.,Kato, T. (登録日: 2019-04-25, 公開日: 2020-02-19, 最終更新日: 2025-07-02)

主引用文献

Yamaguchi, T.,Toma, S.,Terahara, N.,Miyata, T.,Ashihara, M.,Minamino, T.,Namba, K.,Kato, T.
Structural and Functional Comparison ofSalmonellaFlagellar Filaments Composed of FljB and FliC.
Biomolecules, 10:-, 2020

PubMed Abstract: The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. serovar Typhimurium has two genes of flagellin, and , for flagellar filament formation and autonomously switches their expression at a frequency of 10-10 per cell per generation. We report here differences in their structures and motility functions under high-viscosity conditions. A strain expressing FljB showed a higher motility than one expressing FliC under high viscosity. To examine the reasons for this motility difference, we carried out structural analyses of the FljB filament by electron cryomicroscopy and found that the structure was nearly identical to that of the FliC filament except for the position and orientation of the outermost domain D3 of flagellin. The density of domain D3 was much lower in FljB than FliC, suggesting that domain D3 of FljB is more flexible and mobile than that of FliC. These differences suggest that domain D3 plays an important role not only in changing antigenicity of the filament but also in optimizing motility function of the filament as a propeller under different conditions.

PubMed: 32041169
DOI: 10.3390/biom10020246

実験手法

ELECTRON MICROSCOPY (3.56 Å)