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-Structure paper
タイトル | Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT. |
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ジャーナル・号・ページ | Nat Commun, Vol. 12, Issue 1, Page 6508, Year 2021 |
掲載日 | 2021年11月11日 |
![]() | Richard W Meek / James N Blaza / Jil A Busmann / Matthew G Alteen / David J Vocadlo / Gideon J Davies / ![]() ![]() |
PubMed 要旨 | 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. |
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手法 | EM (単粒子) |
解像度 | 5.32 Å |
構造データ | EMDB-12588, PDB-7ntf: |
由来 |
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![]() | TRANSFERASE / O-GlcNAc transferase O-linked B-n-acetylglucosamine transferase |