Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT

• Published in: Nature communications Vol. 12; no. 1; pp. 6508 - 10
• Main Authors: Meek, Richard W., Blaza, James N., Busmann, Jil A., Alteen, Matthew G., Vocadlo, David J., Davies, Gideon J.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 11.11.2021; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 631/45/221; 631/45/607/1172; 631/535/1258/1259; Amino Acids - chemistry; Amino Acids - metabolism; Chromium - chemistry; Chromium - metabolism; Cryoelectron Microscopy - methods; Crystallography; Crystallography, X-Ray; Dimers; Glycomics; Glycosyltransferase; Heterogeneity; Humanities and Social Sciences; Intellectual disabilities; Molecular structure; multidisciplinary; Mutation; Mutation - genetics; N-Acetylglucosamine; Neurodegeneration; Nicotinic Acids - chemistry; Nicotinic Acids - metabolism; O-GlcNAcylation; Protein Structure, Secondary; Proteins; Science; Science (multidisciplinary); X-ray crystallography

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 trans...