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Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation

Nature Structural & Molecular Biology volume 15, pages 764–765 (2008)Cite this article

Abstract

N-Acetylglucosamine (O-GlcNAc) modification of proteins provides a mechanism for the control of diverse cellular processes through a dynamic interplay with phosphorylation. UDP-GlcNAc:polypeptidyl transferase (OGT) catalyzes O-GlcNAc addition. The structure of an intact OGT homolog and kinetic analysis of human OGT variants reveal a contiguous superhelical groove that directs substrates to the active site.

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Figure 1: The three-dimensional structure of XcOGT.
Figure 2: Kinetics of human OGT and its active center variants.

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Acknowledgements

This work was funded by the UK Biotechnology and Biological Sciences Research Council and the the Canadian Institutes of Health Research. G.J.D. is a Royal Society/Wolfson research Merit Award recipient. D.J.V. is a Canada Research Chair in chemical glycobiology and a fellow of the Michael Smith Foundation for Health Research (MSFHR). M.S.M. is a scholar of the MSFHR.

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Authors and Affiliations

  1. Department of Chemistry, Structural Biology Laboratory, The University of York, Heslington, YO10 5YW, York, UK

    Carlos Martinez-Fleites, Yuan He & Gideon J Davies

  2. Department of Chemistry, Simon Fraser University, 8888 University Drive, Burnaby, V5A 1S6, British Columbia, Canada

    Matthew S Macauley, David L Shen & David J Vocadlo

Authors
  1. Carlos Martinez-Fleites
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  2. Matthew S Macauley
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  3. Yuan He
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  4. David L Shen
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  5. David J Vocadlo
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  6. Gideon J Davies
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Corresponding authors

Correspondence to David J Vocadlo or Gideon J Davies.

Supplementary information

Supplementary Text and Figures

Supplementary Figures 1–4, Supplementary Tables 1 and 2, and Supplementary Methods (PDF 5615 kb)

Supplementary Movie 1

Rotating view of the XcOGT (cyan)/Human TPR domain (gold) model with an importin-derived peptide in yellow and UDP in red. (AVI 8436 kb)

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Martinez-Fleites, C., Macauley, M., He, Y. et al. Structure of an O-GlcNAc transferase homolog provides insight into intracellular glycosylation. Nat Struct Mol Biol 15, 764–765 (2008). https://doi.org/10.1038/nsmb.1443

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