PMID:19251647
| Citation |
Pell, LG, Kanelis, V, Donaldson, LW, Howell, PL and Davidson, AR (2009) The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system. Proc. Natl. Acad. Sci. U.S.A. 106:4160-5 |
|---|---|
| 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 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. |
| Links |
PubMed PMC2657425 Online version:10.1073/pnas.0900044106 |
| Keywords |
Bacterial Proteins/chemistry; Bacterial Proteins/secretion; Bacteriophage lambda/chemistry; Biological Evolution; Caudovirales/chemistry; Gram-Negative Bacteria/pathogenicity; Membrane Transport Proteins/chemistry; Protein Conformation; Structural Homology, Protein; Viral Proteins/chemistry |
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