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

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.

journal_name

Nature

journal_title

Nature

authors

Taylor NM,Prokhorov NS,Guerrero-Ferreira RC,Shneider MM,Browning C,Goldie KN,Stahlberg H,Leiman PG

doi

10.1038/nature17971

subject

Has Abstract

pub_date

2016-05-19 00:00:00

pages

346-52

issue

7603

eissn

0028-0836

issn

1476-4687

pii

nature17971

journal_volume

533

pub_type

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