1ZKU

Fitting of the gp9 structure in the EM density of bacteriophage T4 extended tail

Summary for 1ZKU

• Entry DOI: 10.2210/pdb1zku/pdb
• Related: 1PDL 1QEX 1S2E
• EMDB information: 1126
• Descriptor: Baseplate structural protein Gp9, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID (2 entities in total)
• Functional Keywords: structural protein, viral protein
• Biological source: Enterobacteria phage T4
• Total number of polymer chains: 18
• Total formula weight: 562734.54

Authors

Kostyuchenko, V.A. (deposition date: 2005-05-04, release date: 2005-08-09, Last modification date: 2024-02-14)

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., 12:810-813, 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)