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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
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    Citations

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    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. 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.
    3. 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.
    4. 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.
    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.

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