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Structure of the cell-puncturing device of bacteriophage T4

Author

Listed:
  • Shuji Kanamaru

    (Purdue University)

  • Petr G. Leiman

    (Purdue University)

  • Victor A. Kostyuchenko

    (Purdue University
    Laboratory of Molecular Bioengineering, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry)

  • Paul R. Chipman

    (Purdue University)

  • Vadim V. Mesyanzhinov

    (Laboratory of Molecular Bioengineering, Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry)

  • Fumio Arisaka

    (Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology)

  • Michael G. Rossmann

    (Purdue University)

Abstract

Bacteriophage T4 has a very efficient mechanism for infecting cells1. The key component of this process is the baseplate, located at the end of the phage tail, which regulates the interaction of the tail fibres and the DNA ejection machine2. A complex of gene product (gp) 5 (63K) and gp27 (44K), the central part of the baseplate, is required to penetrate the outer cell membrane of Escherichia coli and to disrupt the intermembrane peptidoglycan layer, promoting subsequent entry of phage DNA into the host. We present here a crystal structure of the (gp5–gp27)3 321K complex, determined to 2.9 Å resolution and fitted into a cryo-electron microscopy map at 17 Å resolution of the baseplate-tail tube assembly. The carboxy-terminal domain of gp5 is a triple-stranded β-helix that forms an equilateral triangular prism, which acts as a membrane-puncturing needle. The middle lysozyme domain of gp5, situated on the periphery of the prism, serves to digest the peptidoglycan layer. The amino-terminal, antiparallel β-barrel domain of gp5 is inserted into a cylinder formed by three gp27 monomers, which may serve as a channel for DNA ejection.

Suggested Citation

  • Shuji Kanamaru & Petr G. Leiman & Victor A. Kostyuchenko & Paul R. Chipman & Vadim V. Mesyanzhinov & Fumio Arisaka & Michael G. Rossmann, 2002. "Structure of the cell-puncturing device of bacteriophage T4," Nature, Nature, vol. 415(6871), pages 553-557, January.
    • Handle: RePEc:nat:nature:v:415:y:2002:i:6871:d:10.1038_415553a
    DOI: 10.1038/415553a
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    Cited by:

    1. Ravi R. Sonani & Lee K. Palmer & Nathaniel C. Esteves & Abigail A. Horton & Amanda L. Sebastian & Rebecca J. Kelly & Fengbin Wang & Mark A. B. Kreutzberger & William K. Russell & Petr G. Leiman & Birg, 2024. "An extensive disulfide bond network prevents tail contraction in Agrobacterium tumefaciens phage Milano," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Rong-Cheng Yu & Feng Yang & Hong-Yan Zhang & Pu Hou & Kang Du & Jie Zhu & Ning Cui & Xudong Xu & Yuxing Chen & Qiong Li & Cong-Zhao Zhou, 2024. "Structure of the intact tail machine of Anabaena myophage A-1(L)," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    3. Xiaofei Ge & Jiawei Wang, 2024. "Structural mechanism of bacteriophage lambda tail’s interaction with the bacterial receptor," Nature Communications, Nature, vol. 15(1), pages 1-11, December.

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