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Structure of the substrate-engaged SecA-SecY protein translocation machine

Author

Listed:
  • Chengying Ma

    (Peking University)

  • Xiaofei Wu

    (Peking University)

  • Dongjie Sun

    (Peking University)

  • Eunyong Park

    (University of California-Berkeley)

  • Marco A. Catipovic

    (Howard Hughes Medical Institute and Harvard Medical School)

  • Tom A. Rapoport

    (Howard Hughes Medical Institute and Harvard Medical School)

  • Ning Gao

    (Peking University)

  • Long Li

    (Peking University)

Abstract

The Sec61/SecY channel allows the translocation of many proteins across the eukaryotic endoplasmic reticulum membrane or the prokaryotic plasma membrane. In bacteria, most secretory proteins are transported post-translationally through the SecY channel by the SecA ATPase. How a polypeptide is moved through the SecA-SecY complex is poorly understood, as structural information is lacking. Here, we report an electron cryo-microscopy (cryo-EM) structure of a translocating SecA-SecY complex in a lipid environment. The translocating polypeptide chain can be traced through both SecA and SecY. In the captured transition state of ATP hydrolysis, SecA’s two-helix finger is close to the polypeptide, while SecA’s clamp interacts with the polypeptide in a sequence-independent manner by inducing a short β-strand. Taking into account previous biochemical and biophysical data, our structure is consistent with a model in which the two-helix finger and clamp cooperate during the ATPase cycle to move a polypeptide through the channel.

Suggested Citation

  • Chengying Ma & Xiaofei Wu & Dongjie Sun & Eunyong Park & Marco A. Catipovic & Tom A. Rapoport & Ning Gao & Long Li, 2019. "Structure of the substrate-engaged SecA-SecY protein translocation machine," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-10918-2
    DOI: 10.1038/s41467-019-10918-2
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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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