2BSG

The modeled structure of fibritin (gpwac) of bacteriophage T4 based on cryo-EM reconstruction of the extended tail of bacteriophage T4

Summary for 2BSG

• Entry DOI: 10.2210/pdb2bsg/pdb
• Related: 1AA0 1AVY 1OX3 1RFO 1V1H 1V1I
• EMDB information: 1126
• Descriptor: FIBRITIN (1 entity in total)
• Functional Keywords: viral protein, attachment protein, bacteriophage assembly, bacteriophage t4, chaperone, fibritin, structural protein
• Biological source: BACTERIOPHAGE T4
• Total number of polymer chains: 3
• Total formula weight: 155727.49

Authors

Kostyuchenko, V.A.,Chipman, P.R.,Leiman, P.G.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2005-05-20, release date: 2005-09-21, Last modification date: 2024-05-08)

Primary citation

Kostyuchenko, V.A.,Chipman, P.R.,Leiman, P.G.,Arisaka, F.,Mesyanzhinov, V.V.,Rossmann, M.G.
The Tail Structure of Bacteriophage T4 and its Mechanism of Contraction.
Nat.Struct.Mol.Biol., 12:810-, 2005

PubMed Abstract: Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space.

PubMed: 16116440
DOI: 10.1038/NSMB975

Experimental method

ELECTRON MICROSCOPY (15 Å)