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

Nicholas M. I. Taylor, Nikolai S. Prokhorov, Ricardo C. Guerrero-Ferreira, Mikhail M. Shneider, Christopher Browning, Kenneth N. Goldie, Henning Stahlberg and Petr G. Leiman ()
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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
Ricardo C. Guerrero-Ferreira: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
Mikhail M. Shneider: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
Christopher Browning: École Polytechnique Fédérale de Lausanne (EPFL), BSP-415
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

Nature, 2016, vol. 533, issue 7603, 346-352

Abstract: 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.

Date: 2016
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DOI: 10.1038/nature17971

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