EMD-1086

Single-particle
16.0 Å
EMD-1086 Deposition: 03/06/2004
Map released: 07/09/2004
Last modified: 17/04/2013
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-1086

Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host.

EMD-1086

Single-particle
16.0 Å
EMD-1086 Deposition: 03/06/2004
Map released: 07/09/2004
Last modified: 17/04/2013
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Enterobacteria phage T4
Sample: T4 phages treated with 3 M urea
Fitted models: 1tja, 3j2n, 2fl9, 3foi, 3h3y (Avg. Q-score: 0.0646)

Deposition Authors: Leiman PG , Chipman PR , Kostyuchenko VA , Mesyanzhinov VV, Rossmann MG
Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host.
Leiman PG , Chipman PR , Kostyuchenko VA , Mesyanzhinov VV, Rossmann MG
(2004) Cell , 118 , 419 - 429
Abstract:
The contractile tail of bacteriophage T4 undergoes major structural transitions when the virus attaches to the host cell surface. The baseplate at the distal end of the tail changes from a hexagonal to a star shape. This causes the sheath around the tail tube to contract and the tail tube to protrude from the baseplate and pierce the outer cell membrane and the cell wall before reaching the inner cell membrane for subsequent viral DNA injection. Analogously, the T4 tail can be contracted by treatment with 3 M urea. The structure of the T4 contracted tail, including the head-tail joining region, has been determined by cryo-electron microscopy to 17 A resolution. This 1200 A-long, 20 MDa structure has been interpreted in terms of multiple copies of its approximately 20 component proteins. A comparison with the metastable hexagonal baseplate of the mature virus shows that the baseplate proteins move as rigid bodies relative to each other during the structural change.