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

Taylor, Nicholas M. I. and Prokhorov, Nikolai S. and Guerrero-Ferreira, Ricardo C. and Shneider, Mikhail M. and Browning, Christopher and Goldie, Kenneth N. and Stahlberg, Henning and Leiman, Petr G.. (2016) Structure of the T4 baseplate and its function in triggering sheath contraction. Nature, 533 (7603). pp. 346-352.

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Official URL: http://edoc.unibas.ch/42183/

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Stahlberg)
05 Faculty of Science
UniBasel Contributors:Stahlberg, Henning and Goldie, Kenneth N.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Research
ISSN:0028-0836
e-ISSN:1476-4687
Note:Publication type according to Uni Basel Research Database: Journal article
Identification Number:
Last Modified:01 Oct 2020 14:25
Deposited On:27 Oct 2017 11:46

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