+Search query
-Structure paper
Title | Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 6508, Year 2021 |
Publish date | Nov 11, 2021 |
![]() | Richard W Meek / James N Blaza / Jil A Busmann / Matthew G Alteen / David J Vocadlo / Gideon J Davies / ![]() ![]() |
PubMed Abstract | The O-linked β-N-acetylglucosamine modification is a core signalling mechanism, with erroneous patterns leading to cancer and neurodegeneration. Although thousands of proteins are subject to this ...The O-linked β-N-acetylglucosamine modification is a core signalling mechanism, with erroneous patterns leading to cancer and neurodegeneration. Although thousands of proteins are subject to this modification, only a single essential glycosyltransferase catalyses its installation, the O-GlcNAc transferase, OGT. Previous studies have provided truncated structures of OGT through X-ray crystallography, but the full-length protein has never been observed. Here, we report a 5.3 Å cryo-EM model of OGT. We show OGT is a dimer, providing a structural basis for how some X-linked intellectual disability mutations at the interface may contribute to disease. We observe that the catalytic section of OGT abuts a 13.5 tetratricopeptide repeat unit region and find the relative positioning of these sections deviate from the previously proposed, X-ray crystallography-based model. We also note that OGT exhibits considerable heterogeneity in tetratricopeptide repeat units N-terminal to the dimer interface with repercussions for how OGT binds protein ligands and partners. |
![]() | ![]() ![]() ![]() |
Methods | EM (single particle) |
Resolution | 5.32 Å |
Structure data | EMDB-12588, PDB-7ntf: |
Source |
|
![]() | TRANSFERASE / O-GlcNAc transferase O-linked B-n-acetylglucosamine transferase |