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

Richard W. Meek; James N. Blaza; Jil A. Busmann; Matthew G. Alteen; David J. Vocadlo; Gideon J. Davies

doi:10.1038/s41467-021-26796-6

Nature Communications (Nov 2021)

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

Richard W. Meek,
James N. Blaza,
Jil A. Busmann,
Matthew G. Alteen,
David J. Vocadlo,
Gideon J. Davies

Affiliations

Richard W. Meek: York Structural Biology Laboratory, Department of Chemistry, University of York
James N. Blaza: York Structural Biology Laboratory, Department of Chemistry, University of York
Jil A. Busmann: Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive
Matthew G. Alteen: Department of Chemistry, Simon Fraser University, 8888 University Drive
David J. Vocadlo: Department of Molecular Biology and Biochemistry, Simon Fraser University, 8888 University Drive
Gideon J. Davies: York Structural Biology Laboratory, Department of Chemistry, University of York

DOI: https://doi.org/10.1038/s41467-021-26796-6
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 10

Abstract

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The modification of proteins with O-linked β-N-acetylglucosamine (OGlcNAc) plays roles in regulation of numerous cellular functions while incorrect O-GlcNAcylation patterns are linked to disease. Here, the authors report a cryo-EM structure of full-length O-GlcNAc transferase (OGT), the only enzyme responsible for O-GlcNAcylation.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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