1TJA

Fitting of gp8, gp9, and gp11 into the cryo-EM reconstruction of the bacteriophage T4 contracted tail

Summary for 1TJA

• Entry DOI: 10.2210/pdb1tja/pdb
• Related: 1EL6 1N7Z 1PDF 1PDM 1PDP 1S2E
• EMDB information: 1086
• Descriptor: Baseplate structural protein Gp8, Baseplate structural protein Gp9, Baseplate structural protein Gp11 (3 entities in total)
• Functional Keywords: fitting, docking, cryo-em, gp8, gp9, gp11, circular symmetry, viral protein
• Biological source: Enterobacteria phage T4; More
• Total number of polymer chains: 8
• Total formula weight: 240334.08

Authors

Leiman, P.G.,Chipman, P.R.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2004-06-03, release date: 2004-08-31, Last modification date: 2024-02-14)

Primary citation

Leiman, P.G.,Chipman, P.R.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G.
Three-dimensional rearrangement of proteins in the tail of bacteriophage t4 on infection of its host
Cell(Cambridge,Mass.), 118:419-429, 2004

PubMed 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.

PubMed: 15315755
DOI: 10.1016/j.cell.2004.07.022

Experimental method

ELECTRON MICROSCOPY (16 Å)