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-Structure paper
タイトル | The wild-type flagellar filament of the Firmicute Kurthia at 2.8 Å resolution in vivo. |
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ジャーナル・号・ページ | Sci Rep, Vol. 9, Issue 1, Page 14948, Year 2019 |
掲載日 | 2019年10月18日 |
著者 | Thorsten B Blum / Sevasti Filippidou / Mathilda Fatton / Pilar Junier / Jan Pieter Abrahams / |
PubMed 要旨 | 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 ...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. |
リンク | Sci Rep / PubMed:31628388 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 2.8 Å |
構造データ | EMDB-10362, PDB-6t17: |
由来 |
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キーワード | PROTEIN FIBRIL / Gram-Positive Bacteria Flagella / Helical / Wild-Type |