6P3E

Mobile loops and electrostatic interactions maintain the flexible lambda tail tube


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: HELICAL 

wwPDB Validation 3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Mobile Loops and Electrostatic Interactions Maintain the Flexible Tail Tube of Bacteriophage Lambda.

Campbell, P.L.Duda, R.L.Nassur, J.Conway, J.F.Huet, A.

(2020) J Mol Biol 432: 384-395

  • DOI: 10.1016/j.jmb.2019.10.031
  • Structures With Same Primary Citation

  • 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 bacteri ...

    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.


    Organizational Affiliation

    Department of Biological Sciences, Dietrich School of Arts and Sciences, Pittsburgh, PA 15260, USA; Department of Structural Biology, School of Medicine, University of Pittsburgh, Pittsburgh, PA 15260, USA.



Macromolecules

Find similar proteins by: Sequence  |  Structure

Entity ID: 1
MoleculeChainsSequence LengthOrganismDetails
Tail tube protein
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R
246Escherichia virus LambdaMutation(s): 0 
Gene Names: Vlambdap13
Find proteins for P03733 (Escherichia phage lambda)
Go to UniProtKB:  P03733
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 5.40 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: HELICAL 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)United StatesR01 GM047795
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)United StatesS10 OD019995

Revision History 

  • Version 1.0: 2019-11-27
    Type: Initial release
  • Version 1.1: 2019-12-18
    Changes: Author supporting evidence
  • Version 1.2: 2020-02-12
    Changes: Database references