Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 106, Issue 11, Pages 4160-4165Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0900044106
Keywords
NMR structure; disordered regions; macromolecular assembly
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Funding
- Canadian Institutes of Health Research [MOP-77680, MT13337]
- University of Toronto Open scholarship
- Canadian Cystic Fibrosis Foundation fellowship
- Canada Foundation for Innovation
- Quebec Ministere de la Recherche en Science et Technologie
- McGill University
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Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of the noncontractile phage lambda tail tube. This structure is very similar to a previously solved tail tube protein from a contractile-tailed phage, providing the first direct evidence of an evolutionary connection between these 2 distinct types of phage tails. A remarkable structural similarity is also seen to Hcp1, a component of the bacterial type VI secretion system. The hexameric structure of Hcp1 and its ability to form long tubes are strikingly reminiscent of gpV when it is polymerized into a tail tube. These data coupled with other similarities between phage and type VI secretion proteins support an evolutionary relationship between these systems. Using Hcp1 as a model, we propose a polymerization mechanism for gpV involving several disorder-to-order transitions.
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