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Crystal structure of a substrate-engaged SecY protein-translocation channel

Author

Listed:
  • Long Li

    (Howard Hughes Medical Institute and Harvard Medical School)

  • Eunyong Park

    (Howard Hughes Medical Institute and Harvard Medical School
    †Present address: The Rockefeller University and Howard Hughes Medical Institute, 1230 York Avenue, New York, New York 10065, USA.)

  • JingJing Ling

    (Whitehead Institute for Biomedical Research)

  • Jessica Ingram

    (Whitehead Institute for Biomedical Research)

  • Hidde Ploegh

    (Whitehead Institute for Biomedical Research)

  • Tom A. Rapoport

    (Howard Hughes Medical Institute and Harvard Medical School)

Abstract

The crystal structure of a substrate-engaged SecY channel and the SecA ATPase, which provides molecular insight into the process of protein translocation across membranes.

Suggested Citation

  • Long Li & Eunyong Park & JingJing Ling & Jessica Ingram & Hidde Ploegh & Tom A. Rapoport, 2016. "Crystal structure of a substrate-engaged SecY protein-translocation channel," Nature, Nature, vol. 531(7594), pages 395-399, March.
    • Handle: RePEc:nat:nature:v:531:y:2016:i:7594:d:10.1038_nature17163
    DOI: 10.1038/nature17163
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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.
    2. J. Josephine Botsch & Roswitha Junker & Michèle Sorgenfrei & Patricia P. Ogger & Luca Stier & Susanne Gronau & Peter J. Murray & Markus A. Seeger & Brenda A. Schulman & Bastian Bräuning, 2024. "Doa10/MARCH6 architecture interconnects E3 ligase activity with lipid-binding transmembrane channel to regulate SQLE," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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