Journal
EMBO JOURNAL
Volume 28, Issue 7, Pages 821-829Publisher
WILEY
DOI: 10.1038/emboj.2009.36
Keywords
bacteriophage T4; cryo-electron microscopy; crystallography; tail sheath contraction
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Funding
- National Science Foundation [MCB-0443899]
- a Purdue Research Foundation
- A.A.A
- a Russian Fund for Basic Research [08-04-01260]
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The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central noncontractile tail tube. The contraction of the sheath drives the tail tube through the outer membrane, creating a channel for the viral genome delivery. A crystal structure of about three quarters of gp18 has been determined and was fitted into cryo-electron microscopy reconstructions of the tail sheath before and after contraction. It was shown that during contraction, gp18 subunits slide over each other with no apparent change in their structure.
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