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

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Author Taylor Nicholas M I, Prokhorov Nikolai S, Guerrero-Ferreira Ricardo C, Shneider Mikhail M, Browning Christopher, Goldie Kenneth N, Stahlberg Henning, Leiman Petr G,
Project Electron Microscopy of Membrane Proteins
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Original article (peer-reviewed)

Journal Nature
Volume (Issue) 533(7603)
Page(s) 346 - 52
Title of proceedings Nature
DOI 10.1038/nature17971


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.