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

ABSTRACT: 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

SUBMITTER: Pell LG 

PROVIDER: S-EPMC2657425 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature