IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v555y2018i7696d10.1038_nature25755.html
   My bibliography  Save this article

The atomic structure of a eukaryotic oligosaccharyltransferase complex

Author

Listed:
  • Lin Bai

    (Center for Epigenetics, Van Andel Research Institute)

  • Tong Wang

    (Advanced Science Research Center at the Graduate Center of the City University of New York)

  • Gongpu Zhao

    (David Van Andel Advanced Cryo-Electron Microscopy Suite, Van Andel Research Institute)

  • Amanda Kovach

    (Center for Epigenetics, Van Andel Research Institute)

  • Huilin Li

    (Center for Epigenetics, Van Andel Research Institute)

Abstract

N-glycosylation is a ubiquitous modification of eukaryotic secretory and membrane-bound proteins; about 90% of glycoproteins are N-glycosylated. The reaction is catalysed by an eight-protein oligosaccharyltransferase (OST) complex that is embedded in the endoplasmic reticulum membrane. Our understanding of eukaryotic protein N-glycosylation has been limited owing to the lack of high-resolution structures. Here we report a 3.5 Å resolution cryo-electron microscopy structure of the Saccharomyces cerevisiae OST complex, revealing the structures of subunits Ost1–Ost5, Stt3, Wbp1 and Swp1. We found that seven phospholipids mediate many of the inter-subunit interactions, and an Stt3 N-glycan mediates interactions with Wbp1 and Swp1 in the lumen. Ost3 was found to mediate the OST–Sec61 translocon interface, funnelling the acceptor peptide towards the OST catalytic site as the nascent peptide emerges from the translocon. The structure provides insights into co-translational protein N-glycosylation, and may facilitate the development of small-molecule inhibitors that target this process.

Suggested Citation

  • Lin Bai & Tong Wang & Gongpu Zhao & Amanda Kovach & Huilin Li, 2018. "The atomic structure of a eukaryotic oligosaccharyltransferase complex," Nature, Nature, vol. 555(7696), pages 328-333, March.
  • Handle: RePEc:nat:nature:v:555:y:2018:i:7696:d:10.1038_nature25755
    DOI: 10.1038/nature25755
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature25755
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.

    File URL: https://libkey.io/10.1038/nature25755?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Ana S. Ramírez & Mario Capitani & Giorgio Pesciullesi & Julia Kowal & Joël S. Bloch & Rossitza N. Irobalieva & Jean-Louis Reymond & Markus Aebi & Kaspar P. Locher, 2022. "Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase," Nature Communications, Nature, vol. 13(1), pages 1-12, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:555:y:2018:i:7696:d:10.1038_nature25755. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.