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

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...

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Autores principales:	Richard W. Meek, James N. Blaza, Jil A. Busmann, Matthew G. Alteen, David J. Vocadlo, Gideon J. Davies
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b53d14eee722429eb6788dd3501e0e16
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spelling	oai:doaj.org-article:b53d14eee722429eb6788dd3501e0e162021-11-14T12:36:09ZCryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT10.1038/s41467-021-26796-62041-1723https://doaj.org/article/b53d14eee722429eb6788dd3501e0e162021-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-26796-6https://doaj.org/toc/2041-1723The 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.Richard W. MeekJames N. BlazaJil A. BusmannMatthew G. AlteenDavid J. VocadloGideon J. DaviesNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Richard W. Meek James N. Blaza Jil A. Busmann Matthew G. Alteen David J. Vocadlo Gideon J. Davies Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
description	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.
format	article
author	Richard W. Meek James N. Blaza Jil A. Busmann Matthew G. Alteen David J. Vocadlo Gideon J. Davies
author_facet	Richard W. Meek James N. Blaza Jil A. Busmann Matthew G. Alteen David J. Vocadlo Gideon J. Davies
author_sort	Richard W. Meek
title	Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
title_short	Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
title_full	Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
title_fullStr	Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
title_full_unstemmed	Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT
title_sort	cryo-em structure provides insights into the dimer arrangement of the o-linked β-n-acetylglucosamine transferase ogt
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/b53d14eee722429eb6788dd3501e0e16
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Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT

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