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Structure of the T4 baseplate and its function in triggering sheath contraction

Author

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  • Nicholas M. I. Taylor

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415)

  • Nikolai S. Prokhorov

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
    Winogradsky Institute of Microbiology, Research Center of Biotechnology of the Russian Academy of Sciences)

  • Ricardo C. Guerrero-Ferreira

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415)

  • Mikhail M. Shneider

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
    Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Laboratory of Molecular Bioengineering)

  • Christopher Browning

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
    †Present address: Vertex Pharmaceuticals (Europe) Ltd, 86–88 Jubilee Avenue, Milton Park, Abingdon, Oxfordshire OX14 4RW, UK.)

  • Kenneth N. Goldie

    (Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel)

  • Henning Stahlberg

    (Center for Cellular Imaging and NanoAnalytics (C-CINA), Biozentrum, University of Basel)

  • Petr G. Leiman

    (École Polytechnique Fédérale de Lausanne (EPFL), BSP-415)

Abstract

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.

Suggested Citation

  • Nicholas M. I. Taylor & Nikolai S. Prokhorov & Ricardo C. Guerrero-Ferreira & Mikhail M. Shneider & Christopher Browning & Kenneth N. Goldie & Henning Stahlberg & Petr G. Leiman, 2016. "Structure of the T4 baseplate and its function in triggering sheath contraction," Nature, Nature, vol. 533(7603), pages 346-352, May.
    • Handle: RePEc:nat:nature:v:533:y:2016:i:7603:d:10.1038_nature17971
    DOI: 10.1038/nature17971
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