IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v469y2011i7331d10.1038_nature09638.html
   My bibliography  Save this article

Structure of human O-GlcNAc transferase and its complex with a peptide substrate

Author

Listed:
  • Michael B. Lazarus

    (Harvard University
    Harvard Medical School)

  • Yunsun Nam

    (Harvard Medical School
    Laboratory of Molecular Medicine, Children’s Hospital)

  • Jiaoyang Jiang

    (Harvard Medical School)

  • Piotr Sliz

    (Harvard Medical School
    Laboratory of Molecular Medicine, Children’s Hospital)

  • Suzanne Walker

    (Harvard Medical School)

Abstract

Structure of a nutrient sensor O-GlcNAc transferase (OGT) is an essential mammalian enzyme that acts as a nutrient sensor. It glycosylates proteins with O-linked β-N-acetylglucosamine (O-GlcNAc), and this regulates a variety of cellular signalling pathways. Suzanne Walker and colleagues present the crystal structure of human OGT as a binary complex with UDP and as a ternary complex with UDP and a peptide substrate. The structures show how OGT recognizes peptide sequences, and provide information on the mechanism of action of an enzyme that has been found in aberrant form in a number of human conditions including diabetes, cancer and Alzheimer's disease.

Suggested Citation

  • Michael B. Lazarus & Yunsun Nam & Jiaoyang Jiang & Piotr Sliz & Suzanne Walker, 2011. "Structure of human O-GlcNAc transferase and its complex with a peptide substrate," Nature, Nature, vol. 469(7331), pages 564-567, January.
    • Handle: RePEc:nat:nature:v:469:y:2011:i:7331:d:10.1038_nature09638
    DOI: 10.1038/nature09638
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09638
    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/nature09638?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. Richard W. Meek & James N. Blaza & Jil A. Busmann & Matthew G. Alteen & David J. Vocadlo & Gideon J. Davies, 2021. "Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Shivesh Kumar & Yan Wang & Ye Zhou & Lucas Dillard & Fay-Wei Li & Carly A. Sciandra & Ning Sui & Rodolfo Zentella & Emily Zahn & Jeffrey Shabanowitz & Donald F. Hunt & Mario J. Borgnia & Alberto Barte, 2023. "Structure and dynamics of the Arabidopsis O-fucosyltransferase SPINDLY," Nature Communications, Nature, vol. 14(1), pages 1-12, December.
    3. Shiyang Cao & Tong Wang & Yifan Ren & Gengshan Wu & Yuan Zhang & Yafang Tan & Yazhou Zhou & Hongyan Chen & Yu Zhang & Yajun Song & Ruifu Yang & Zongmin Du, 2024. "A protein O-GlcNAc glycosyltransferase regulates the antioxidative response in Yersinia pestis," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Duc T. Huynh & Kalina N. Tsolova & Abigail J. Watson & Sai Kwan Khal & Jordan R. Green & Di Li & Jimin Hu & Erik J. Soderblom & Jen-Tsan Chi & Chantell S. Evans & Michael Boyce, 2023. "O-GlcNAcylation regulates neurofilament-light assembly and function and is perturbed by Charcot-Marie-Tooth disease mutations," Nature Communications, Nature, vol. 14(1), pages 1-17, December.
    5. Ping Lu & Yusong Liu & Maozhou He & Ting Cao & Mengquan Yang & Shutao Qi & Hongtao Yu & Haishan Gao, 2023. "Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex," Nature Communications, Nature, vol. 14(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:469:y:2011:i:7331:d:10.1038_nature09638. 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.