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Structure of the bacteriophage φ29 DNA packaging motor

Author

Listed:
  • Alan A. Simpson

    (Purdue University)

  • Yizhi Tao

    (Purdue University
    Harvard University)

  • Petr G. Leiman

    (Purdue University)

  • Mohammed O. Badasso

    (18-246 Moos Tower, University of Minnesota)

  • Yongning He

    (Purdue University)

  • Paul J. Jardine

    (University of New Brunswick)

  • Norman H. Olson

    (Purdue University)

  • Marc C. Morais

    (Purdue University)

  • Shelley Grimes

    (18-246 Moos Tower, University of Minnesota)

  • Dwight L. Anderson

    (18-246 Moos Tower, University of Minnesota)

  • Timothy S. Baker

    (Purdue University)

  • Michael G. Rossmann

    (Purdue University)

Abstract

Motors generating mechanical force, powered by the hydrolysis of ATP, translocate double-stranded DNA into preformed capsids (proheads) of bacterial viruses1,2 and certain animal viruses3. Here we describe the motor that packages the double-stranded DNA of the Bacillus subtilis bacteriophage φ29 into a precursor capsid. We determined the structure of the head–tail connector—the central component of the φ29 DNA packaging motor—to 3.2 Å resolution by means of X-ray crystallography. We then fitted the connector into the electron densities of the prohead and of the partially packaged prohead as determined using cryo-electron microscopy and image reconstruction analysis. Our results suggest that the prohead plus dodecameric connector, prohead RNA, viral ATPase and DNA comprise a rotary motor with the head–prohead RNA–ATPase complex acting as a stator, the DNA acting as a spindle, and the connector as a ball-race. The helical nature of the DNA converts the rotary action of the connector into translation of the DNA.

Suggested Citation

  • Alan A. Simpson & Yizhi Tao & Petr G. Leiman & Mohammed O. Badasso & Yongning He & Paul J. Jardine & Norman H. Olson & Marc C. Morais & Shelley Grimes & Dwight L. Anderson & Timothy S. Baker & Michael, 2000. "Structure of the bacteriophage φ29 DNA packaging motor," Nature, Nature, vol. 408(6813), pages 745-750, December.
    • Handle: RePEc:nat:nature:v:408:y:2000:i:6813:d:10.1038_35047129
    DOI: 10.1038/35047129
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    Cited by:

    1. Igor Orlov & Stéphane Roche & Sandrine Brasilès & Natalya Lukoyanova & Marie-Christine Vaney & Paulo Tavares & Elena V. Orlova, 2022. "CryoEM structure and assembly mechanism of a bacterial virus genome gatekeeper," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Hang Yin & Xuzichao Li & Xiaoshen Wang & Chendi Zhang & Jiaqi Gao & Guimei Yu & Qiuqiu He & Jie Yang & Xiang Liu & Yong Wei & Zhuang Li & Heng Zhang, 2024. "Insights into the modulation of bacterial NADase activity by phage proteins," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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