Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)

POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme’s subst...

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Autores principales:	Zhijie Li, Michael Fischer, Malathy Satkunarajah, Dongxia Zhou, Stephen G. Withers, James M. Rini
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/7319d160abf34c1da5150afd1e429e25
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spelling	oai:doaj.org-article:7319d160abf34c1da5150afd1e429e252021-12-02T14:16:04ZStructural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)10.1038/s41467-017-00255-72041-1723https://doaj.org/article/7319d160abf34c1da5150afd1e429e252017-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-00255-7https://doaj.org/toc/2041-1723POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme’s substrate specificity and catalytic mechanismZhijie LiMichael FischerMalathy SatkunarajahDongxia ZhouStephen G. WithersJames M. RiniNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-12 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Zhijie Li Michael Fischer Malathy Satkunarajah Dongxia Zhou Stephen G. Withers James M. Rini Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
description	POGLUT1 is a protein-O-glucosyltransferase that transfers glucose and xylose to the EGF-like domains of Notch and other signaling receptors. Here the authors report the structure of human POGLUT1 in complexes with 3 different EGF-like domains and donor substrates and shed light on the enzyme’s substrate specificity and catalytic mechanism
format	article
author	Zhijie Li Michael Fischer Malathy Satkunarajah Dongxia Zhou Stephen G. Withers James M. Rini
author_facet	Zhijie Li Michael Fischer Malathy Satkunarajah Dongxia Zhou Stephen G. Withers James M. Rini
author_sort	Zhijie Li
title	Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
title_short	Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
title_full	Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
title_fullStr	Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
title_full_unstemmed	Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)
title_sort	structural basis of notch o-glucosylation and o–xylosylation by mammalian protein–o-glucosyltransferase 1 (poglut1)
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/7319d160abf34c1da5150afd1e429e25
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Structural basis of Notch O-glucosylation and O–xylosylation by mammalian protein–O-glucosyltransferase 1 (POGLUT1)

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