4.8 Article

The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

Publisher

NATL ACAD SCIENCES
DOI: 10.1073/pnas.0900044106

Keywords

NMR structure; disordered regions; macromolecular assembly

Funding

  1. Canadian Institutes of Health Research [MOP-77680, MT13337]
  2. University of Toronto Open scholarship
  3. Canadian Cystic Fibrosis Foundation fellowship
  4. Canada Foundation for Innovation
  5. Quebec Ministere de la Recherche en Science et Technologie
  6. McGill University

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available