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-Structure paper
タイトル | Structure of the T4 baseplate and its function in triggering sheath contraction. |
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ジャーナル・号・ページ | Nature, Vol. 533, Issue 7603, Page 346-352, Year 2016 |
掲載日 | 2016年5月19日 |
著者 | Nicholas M I Taylor / Nikolai S Prokhorov / Ricardo C Guerrero-Ferreira / Mikhail M Shneider / Christopher Browning / Kenneth N Goldie / Henning Stahlberg / Petr G Leiman / |
PubMed 要旨 | Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This ...Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved. |
リンク | Nature / PubMed:27193680 |
手法 | EM (単粒子) / X線回折 |
解像度 | 2.47 - 6.77 Å |
構造データ | EMDB-3374, PDB-5iv5: EMDB-3392: EMDB-3393: EMDB-3394: EMDB-3395: EMDB-3396, PDB-5iv7: EMDB-3397: PDB-5iw9: |
化合物 | ChemComp-ZN: ChemComp-FE: ChemComp-HOH: |
由来 |
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キーワード | VIRAL PROTEIN / T4 / baseplate-tail tube complex / pre-attachment / bacteriophage / bacterial virus / hexagonal / membrane-piercing / cell attachment / infection / baseplate / post-attachment / star-shaped / hubless / contractile sheath / wedge / sheath polymerization |