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Protruding knob-like proteins violate local symmetries in an icosahedral marine virus

Author

Listed:
  • Preeti Gipson

    (Baylor College of Medicine)

  • Matthew L. Baker

    (Baylor College of Medicine)

  • Desislava Raytcheva

    (Northeastern University
    Massachusetts Institute of Technology)

  • Cameron Haase-Pettingell

    (Massachusetts Institute of Technology)

  • Jacqueline Piret

    (Northeastern University)

  • Jonathan A. King

    (Massachusetts Institute of Technology)

  • Wah Chiu

    (Baylor College of Medicine)

Abstract

Marine viruses play crucial roles in shaping the dynamics of oceanic microbial communities and in the carbon cycle on Earth. Here we report a 4.7-Å structure of a cyanobacterial virus, Syn5, by electron cryo-microscopy and modelling. A Cα backbone trace of the major capsid protein (gp39) reveals a classic phage protein fold. In addition, two knob-like proteins protruding from the capsid surface are also observed. Using bioinformatics and structure analysis tools, these proteins are identified to correspond to gp55 and gp58 (each with two copies per asymmetric unit). The non 1:1 stoichiometric distribution of gp55/58 to gp39 breaks all expected local symmetries and leads to non-quasi-equivalence of the capsid subunits, suggesting a role in capsid stabilization. Such a structural arrangement has not yet been observed in any known virus structures.

Suggested Citation

  • Preeti Gipson & Matthew L. Baker & Desislava Raytcheva & Cameron Haase-Pettingell & Jacqueline Piret & Jonathan A. King & Wah Chiu, 2014. "Protruding knob-like proteins violate local symmetries in an icosahedral marine virus," Nature Communications, Nature, vol. 5(1), pages 1-11, September.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms5278
    DOI: 10.1038/ncomms5278
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    Cited by:

    1. Lanlan Cai & Hang Liu & Wen Zhang & Shiwei Xiao & Qinglu Zeng & Shangyu Dang, 2023. "Cryo-EM structure of cyanophage P-SCSP1u offers insights into DNA gating and evolution of T7-like viruses," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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