7NTF

Cryo-EM structure of unliganded O-GlcNAc transferase

7NTF の概要

• エントリーDOI: 10.2210/pdb7ntf/pdb
• EMDBエントリー: 12588
• 分子名称: Isoform 1 of UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit (1 entity in total)
• 機能のキーワード: o-glcnac transferase o-linked b-n-acetylglucosamine transferase, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 240451.55

構造登録者

Meek, R.W.,Blaza, J.N.,Davies, G.J. (登録日: 2021-03-09, 公開日: 2021-11-17, 最終更新日: 2024-07-10)

主引用文献

Meek, R.W.,Blaza, J.N.,Busmann, J.A.,Alteen, M.G.,Vocadlo, D.J.,Davies, G.J.
Cryo-EM structure provides insights into the dimer arrangement of the O-linked beta-N-acetylglucosamine transferase OGT.
Nat Commun, 12:6508-6508, 2021

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 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.

PubMed: 34764280
DOI: 10.1038/s41467-021-26796-6

実験手法

ELECTRON MICROSCOPY (5.32 Å)