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| Title | Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda. |
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| Journal, issue, pages | J Mol Biol, Vol. 432, Issue 2, Page 384-395, Year 2020 |
| Publish date | Jan 17, 2020 |
 Authors | Patricia L Campbell / Robert L Duda / Jamie Nassur / James F Conway / Alexis Huet /  |
| PubMed Abstract | The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. On infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage ...The long flexible tail tube of bacteriophage lambda connects its capsid to the tail tip. On infection, a DNA ejection signal is passed from the tip, along the tube to the capsid that triggers passage of the DNA down the tube and into the host bacterium. The tail tube is built from repeating units of the major tail protein, gpV, which has two distinctive domains. Its N-terminal domain has the same fold as proteins that form the rigid inner tubes of contractile tail phages, such as T4, and its C-terminal domain adopt an Ig-like fold of unknown function. We determined structures of the lambda tail tube in free tails and in virions before and after DNA ejection using cryoelectron microscopy. Modeling of the density maps reveals how electrostatic interactions and a mobile loop participate in assembly and also impart flexibility to the tube while maintaining its integrity. We also demonstrate how a common protein fold produces rigid tubes in some phages but flexible tubes in others. |
 External links | J Mol Biol / PubMed:31711962 / PubMed Central |
| Methods | EM (helical sym.) |
| Resolution | 5.4 - 6.8 Å |
| Structure data | EMDB-20241, PDB-6p3e:  EMDB-20242:  EMDB-20243: |
| Source |
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 Keywords | VIRAL PROTEIN / Tail tube / siphoviridae / helical |
escherichia phage lambda (virus)