2K4Q

The Solution Structure of gpV, the Major Tail Protein from Bacteriophage Lambda

Summary for 2K4Q

• Entry DOI: 10.2210/pdb2k4q/pdb
• NMR Information: BMRB: 15807
• Descriptor: Major tail protein V (1 entity in total)
• Functional Keywords: gpv, bacteriophage lambda, major tail protein, viral protein
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 1
• Total formula weight: 16896.77

Authors

Pell, L.G.,Kanelis, V.,Howell, P.,Davidson, A.R. (deposition date: 2008-06-16, release date: 2009-02-17, Last modification date: 2024-05-08)

Primary citation

Pell, L.G.,Kanelis, V.,Donaldson, L.W.,Howell, P.L.,Davidson, A.R.
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.USA, 106:4160-4165, 2009

PubMed 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.

PubMed: 19251647
DOI: 10.1073/pnas.0900044106

Experimental method

SOLUTION NMR