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-Structure paper
タイトル | Structural and Functional Comparison of Flagellar Filaments Composed of FljB and FliC. |
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ジャーナル・号・ページ | Biomolecules, Vol. 10, Issue 2, Year 2020 |
掲載日 | 2020年2月6日 |
著者 | Tomoko Yamaguchi / Shoko Toma / Naoya Terahara / Tomoko Miyata / Masamichi Ashihara / Tohru Minamino / Keiichi Namba / Takayuki Kato / |
PubMed 要旨 | 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 ...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. |
リンク | Biomolecules / PubMed:32041169 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 3.56 Å |
構造データ | EMDB-0980: |
由来 |
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キーワード | PROTEIN FIBRIL / FljB / Helical reconstruction / Salmonella / Flagellar motor |