Publication Abstract from PubMed
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.
The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system.,Pell LG, Kanelis V, Donaldson LW, Howell PL, Davidson AR Proc Natl Acad Sci U S A. 2009 Mar 17;106(11):4160-5. Epub 2009 Feb 27. PMID:19251647[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
