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

Nicholas M I Taylor, Nikolai Prokhorov, Ricardo C. Guerrero-Ferreira, Mikhail M. Shneider, Christopher Browning, Kenneth N. Goldie, Henning Stahlberg, Petr Leiman

Research output: Contribution to journalArticle

117 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)346-352
Number of pages7
JournalNature
Volume533
DOIs
StatePublished - May 18 2016
Externally publishedYes

ASJC Scopus subject areas

  • General
  • Medicine(all)

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    Taylor, N. M. I., Prokhorov, N., Guerrero-Ferreira, R. C., Shneider, M. M., Browning, C., Goldie, K. N., Stahlberg, H., & Leiman, P. (2016). Structure of the T4 baseplate and its function in triggering sheath contraction. Nature, 533, 346-352. https://doi.org/10.1038/nature17971