5IW9

Structure of bacteriophage T4 gp25, sheath polymerization initiator

Replaces:  4HRZ

Summary for 5IW9

• Entry DOI: 10.2210/pdb5iw9/pdb
• Descriptor: Baseplate wedge protein gp25 (2 entities in total)
• Functional Keywords: contractile sheath, baseplate, wedge, sheath polymerization, viral protein
• Biological source: Enterobacteria phage T4
• Cellular location: Virion : P09425
• Total number of polymer chains: 2
• Total formula weight: 30241.18

Authors

Leiman, P.G.,Browning, C.,Shneider, M.M. (deposition date: 2016-03-22, release date: 2016-05-11, Last modification date: 2024-11-20)

Primary citation

Taylor, N.M.,Prokhorov, N.S.,Guerrero-Ferreira, R.C.,Shneider, M.M.,Browning, C.,Goldie, K.N.,Stahlberg, H.,Leiman, P.G.
Structure of the T4 baseplate and its function in triggering sheath contraction.
Nature, 533:346-352, 2016

PubMed 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.

PubMed: 27193680
DOI: 10.1038/nature17971

Experimental method

X-RAY DIFFRACTION (2.47 Å)