Structure of the T4 baseplate and its function in triggering sheath contraction
Research output: Contribution to journal › Journal article › Research › peer-review
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.
|Number of pages||7|
|Publication status||Published - 2016|
- Bacteriophage T4/chemistry, Cryoelectron Microscopy, Crystallography, X-Ray, Models, Molecular, Protein Conformation, Viral Structural Proteins/chemistry