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Structure of the SecY channel during initiation of protein translocation

Author

Listed:
  • Eunyong Park

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Jean-François Ménétret

    (Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118-2526, USA)

  • James C. Gumbart

    (School of Physics, Georgia Institute of Technology)

  • Steven J. Ludtke

    (National Center for Macromolecular Imaging, Baylor College of Medicine, 1 Baylor Plaza, Houston, Texas 77030, USA)

  • Weikai Li

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Andrew Whynot

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Tom A. Rapoport

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Christopher W. Akey

    (Boston University School of Medicine, 700 Albany Street, Boston, Massachusetts 02118-2526, USA)

Abstract

Newly synthesized proteins are targeted to the SecY protein-conducting channel for translocation across the membrane; here, cryo-electron microscopy structures of inactive and active ribosome–channel complexes are presented, revealing that ribosome binding does not result in major structural changes to transmembrane regions of the channel, and that stable channel opening requires loop insertion of the translocating nascent chain.

Suggested Citation

  • Eunyong Park & Jean-François Ménétret & James C. Gumbart & Steven J. Ludtke & Weikai Li & Andrew Whynot & Tom A. Rapoport & Christopher W. Akey, 2014. "Structure of the SecY channel during initiation of protein translocation," Nature, Nature, vol. 506(7486), pages 102-106, February.
    • Handle: RePEc:nat:nature:v:506:y:2014:i:7486:d:10.1038_nature12720
    DOI: 10.1038/nature12720
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    Cited by:

    1. Zikun Zhu & Shuai Wang & Shu-ou Shan, 2022. "Ribosome profiling reveals multiple roles of SecA in cotranslational protein export," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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