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-Structure paper
タイトル | Atomic Structure of the Francisella T6SS Central Spike Reveals a Unique α-Helical Lid and a Putative Cargo. |
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ジャーナル・号・ページ | Structure, Vol. 27, Issue 12, Page 1811-11819.e6, Year 2019 |
掲載日 | 2019年12月3日 |
著者 | Xue Yang / Daniel L Clemens / Bai-Yu Lee / Yanxiang Cui / Z Hong Zhou / Marcus A Horwitz / |
PubMed 要旨 | Francisella bacteria rely on a phylogenetically distinct type VI secretion system (T6SS) to escape host phagosomes and cause the fatal disease tularemia, but the structural and molecular mechanisms ...Francisella bacteria rely on a phylogenetically distinct type VI secretion system (T6SS) to escape host phagosomes and cause the fatal disease tularemia, but the structural and molecular mechanisms involved are unknown. Here we report the atomic structure of the Francisella T6SS central spike complex, obtained by cryo-electron microscopy. Our structural and functional studies demonstrate that, unlike the single-protein spike composition of other T6SS subtypes, Francisella T6SS's central spike is formed by two proteins, PdpA and VgrG, akin to T4-bacteriophage gp27 and gp5, respectively, and that PdpA has unique characteristics, including a putative cargo within its cavity and an N-terminal helical lid. Structure-guided mutagenesis demonstrates that the PdpA N-terminal lid and C-terminal spike are essential to Francisella T6SS function. PdpA is thus both an adaptor, connecting VgrG to the tube, and a likely carrier of secreted cargo. These findings are important to understanding Francisella pathogenicity and designing therapeutics to combat tularemia. |
リンク | Structure / PubMed:31677891 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.98 - 4.35 Å |
構造データ | EMDB-20695, PDB-6u9e: EMDB-20696, PDB-6u9f: EMDB-20698, PDB-6u9g: |
由来 |
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キーワード | TRANSPORT PROTEIN / T6SS Central Spike / Complex / Type VI Secretion System |