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The tail structure of bacteriophage T4 and its mechanism of contraction

Nature Structural & Molecular Biology volume 12, pages 810–813 (2005)Cite this article

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-Å 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°, allowing it to cross the host's periplasmic space.

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Figure 1: Stereo diagram of bacteriophage T4 showing the extended tail, the LTFs, the neck and a small part of the capsid.
Figure 2: The neck and collar of bacteriophage T4.
Figure 3: The structure of the collar and whiskers.
Figure 4: Conformational changes in the tail sheath.
Figure 5: A helical strand of gp18 in the extended (green) and contracted (brown) tail.

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Acknowledgements

We thank S. Wilder and C. Towell for help in the preparation of the manuscript. The work was supported by a US National Science Foundation grant to M.G.R., a Howard Hughes Medical Institute grant and a Russian Fund for Basic Research grant to V.V.M., a Human Frontiers Science Program grant to M.G.R., F.A. and V.V.M., a Keck Foundation grant to M.G.R. for the purchase of the Philips CM300 field emission gun microscope and a reinvestment grant from Purdue University.

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Authors and Affiliations

  1. Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, 47907-2054, Indiana, USA

    Victor A Kostyuchenko, Paul R Chipman, Petr G Leiman & Michael G Rossmann

  2. Graduate School and School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Yokohama, 226-8501, Japan

    Fumio Arisaka

  3. Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 16/10 Miklukho-Maklaya str., Moscow, 117997, Russia

    Vadim V Mesyanzhinov

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  1. Victor A Kostyuchenko
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Correspondence to Michael G Rossmann.

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Kostyuchenko, V., Chipman, P., Leiman, P. et al. The tail structure of bacteriophage T4 and its mechanism of contraction. Nat Struct Mol Biol 12, 810–813 (2005). https://doi.org/10.1038/nsmb975

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