3FO8

Crystal structure of the bacteriophage T4 tail sheath protein, protease resistant fragment gp18PR

Summary for 3FO8

• Entry DOI: 10.2210/pdb3fo8/pdb
• Related: 3FOA 3FOH 3FOI
• Descriptor: Tail sheath protein Gp18, ACETATE ION (3 entities in total)
• Functional Keywords: mostly beta, viral structural protein, bacteriophage t4, tail sheath, viral protein
• Biological source: Enterobacteria phage T4 (Bacteriophage T4)
• Cellular location: Virion : P13332
• Total number of polymer chains: 1
• Total formula weight: 29946.45

Authors

Aksyuk, A.A.,Leiman, P.G.,Kurochkina, L.P.,Shneider, M.M.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G. (deposition date: 2008-12-29, release date: 2009-03-10, Last modification date: 2024-02-21)

Primary citation

Aksyuk, A.A.,Leiman, P.G.,Kurochkina, L.P.,Shneider, M.M.,Kostyuchenko, V.A.,Mesyanzhinov, V.V.,Rossmann, M.G.
The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria.
Embo J., 28:821-829, 2009

PubMed Abstract: The contractile tail of bacteriophage T4 is a molecular machine that facilitates very high viral infection efficiency. Its major component is a tail sheath, which contracts during infection to less than half of its initial length. The sheath consists of 138 copies of the tail sheath protein, gene product (gp) 18, which surrounds the central non-contractile tail tube. The contraction of the sheath drives the tail tube through the outer membrane, creating a channel for the viral genome delivery. A crystal structure of about three quarters of gp18 has been determined and was fitted into cryo-electron microscopy reconstructions of the tail sheath before and after contraction. It was shown that during contraction, gp18 subunits slide over each other with no apparent change in their structure.

PubMed: 19229296
DOI: 10.1038/emboj.2009.36

Experimental method

X-RAY DIFFRACTION (1.8 Å)