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  • Structure Watch
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Structure watch

Nature Reviews Molecular Cell Biology volume 12, page 138 (2011)Cite this article

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In eukaryotes, metabolic status can be detected and transduced to downstream signalling pathways by O-GlcNAc transferase (OGT). This detects glucose levels by sensing the levels of UDP-GlcNAc, which it then uses to modify downstream targets, including insulin signalling proteins and transcription factors regulating gluconeogenesis, with O-GlcNAc.

OGT is made up of a series of tetratricopeptide repeats (TPR; which are thought to mediate protein–protein interactions) and a catalytic region that had not been structurally resolved. Lazarus et al. report two structures of OGT that provide insight into substrate binding and the enzyme's catalytic mechanism. First, they resolved a structure of OGT–UDP that includes the catalytic region. This region comprises an amino-terminal and a carboxy-terminal domain that are separated by an intermediate domain, which is present only in metazoans and has a unique fold. Next, they obtained a structure of OGT–UDP with peptide. The structure revealed that OGT shows preference for Ser or Thr that are flanked by residues which enforce an extended conformation of the amino acid. The OGT substrates bind in an ordered manner to a cleft between the TPR domain and the catalytic region, access to which is controlled by the TPR domain through an unknown molecular mechanism.

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ORIGINAL RESEARCH PAPERS

  1. Lazarus, M. B. et al. Structure of human O-GlcNAc transferase and its complex with a peptide substrate. Nature 469, 564–567 (2011)

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  2. Böcking, T. et al. Single-molecule analysis of a molecular disassemblase reveals the mechanims of Hsc70-driven clathrin uncoating. Nature Struct. Mol. Biol. 30 Jan 2011 (doi:10.1038/nsmb.1985)

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Structure watch. Nat Rev Mol Cell Biol 12, 138 (2011). https://doi.org/10.1038/nrm3074

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