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-Structure paper
タイトル | A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel. |
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ジャーナル・号・ページ | Nat Microbiol, Vol. 3, Issue 6, Page 678-686, Year 2018 |
掲載日 | 2018年5月21日 |
著者 | David Chetrit / Bo Hu / Peter J Christie / Craig R Roy / Jun Liu / |
PubMed 要旨 | Type IV secretion systems (T4SSs) are complex machines used by bacteria to deliver protein and DNA complexes into target host cells. Conserved ATPases are essential for T4SS function, but how they ...Type IV secretion systems (T4SSs) are complex machines used by bacteria to deliver protein and DNA complexes into target host cells. Conserved ATPases are essential for T4SS function, but how they coordinate their activities to promote substrate transfer remains poorly understood. Here, we show that the DotB ATPase associates with the Dot-Icm T4SS at the Legionella cell pole through interactions with the DotO ATPase. The structure of the Dot-Icm apparatus was solved in situ by cryo-electron tomography at 3.5 nm resolution and the cytoplasmic complex was solved at 3.0 nm resolution. These structures revealed a cell envelope-spanning channel that connects to the cytoplasmic complex. Further analysis revealed a hexameric assembly of DotO dimers associated with the inner membrane complex, and a DotB hexamer associated with the base of this cytoplasmic complex. The assembly of a DotB-DotO energy complex creates a cytoplasmic channel that directs the translocation of substrates through the T4SS. These data define distinct stages in Dot-Icm machine biogenesis, advance our understanding of channel activation, and identify an envelope-spanning T4SS channel. |
リンク | Nat Microbiol / PubMed:29784975 / PubMed Central |
手法 | EM (サブトモグラム平均) |
解像度 | 33.0 Å |
構造データ | EMDB-7611: EMDB-7612: |
由来 |
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