6P3E

Mobile loops and electrostatic interactions maintain the flexible lambda tail tube

Summary for 6P3E

• Entry DOI: 10.2210/pdb6p3e/pdb
• EMDB information: 20241 20242 20243
• Descriptor: Tail tube protein (1 entity in total)
• Functional Keywords: tail tube, siphoviridae, helical, viral protein
• Biological source: Escherichia phage lambda
• Total number of polymer chains: 18
• Total formula weight: 464972.02

Authors

Campbell, P.,Duda, R.L.,Nassur, J.,Hendrix, R.W.,Conway, J.F.,Huet, A. (deposition date: 2019-05-23, release date: 2019-11-27, Last modification date: 2024-03-20)

Primary citation

Campbell, P.L.,Duda, R.L.,Nassur, J.,Conway, J.F.,Huet, A.
Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda.
J.Mol.Biol., 432:384-395, 2020

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 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.

PubMed: 31711962
DOI: 10.1016/j.jmb.2019.10.031

Experimental method

ELECTRON MICROSCOPY (5.4 Å)