Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase

The glycosyltransferase PglH transfers three terminal N-acetylgalactosamine (GalNAc) residues to a carrier, which is a prerequisite for bacterial protein N-glycosylation. Here authors present the crystal structures of PglH in three distinct states and show that a ‘ruler helix’ facilitates membrane a...

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Autores principales:	Ana S. Ramírez, Jérémy Boilevin, Ahmad Reza Mehdipour, Gerhard Hummer, Tamis Darbre, Jean-Louis Reymond, Kaspar P. Locher
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/02fd06bf76d44363ac10479a0e87396b
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spelling	oai:doaj.org-article:02fd06bf76d44363ac10479a0e87396b2021-12-02T14:40:55ZStructural basis of the molecular ruler mechanism of a bacterial glycosyltransferase10.1038/s41467-018-02880-22041-1723https://doaj.org/article/02fd06bf76d44363ac10479a0e87396b2018-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-02880-2https://doaj.org/toc/2041-1723The glycosyltransferase PglH transfers three terminal N-acetylgalactosamine (GalNAc) residues to a carrier, which is a prerequisite for bacterial protein N-glycosylation. Here authors present the crystal structures of PglH in three distinct states and show that a ‘ruler helix’ facilitates membrane attachment and glycan counting.Ana S. RamírezJérémy BoilevinAhmad Reza MehdipourGerhard HummerTamis DarbreJean-Louis ReymondKaspar P. LocherNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ana S. Ramírez Jérémy Boilevin Ahmad Reza Mehdipour Gerhard Hummer Tamis Darbre Jean-Louis Reymond Kaspar P. Locher Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
description	The glycosyltransferase PglH transfers three terminal N-acetylgalactosamine (GalNAc) residues to a carrier, which is a prerequisite for bacterial protein N-glycosylation. Here authors present the crystal structures of PglH in three distinct states and show that a ‘ruler helix’ facilitates membrane attachment and glycan counting.
format	article
author	Ana S. Ramírez Jérémy Boilevin Ahmad Reza Mehdipour Gerhard Hummer Tamis Darbre Jean-Louis Reymond Kaspar P. Locher
author_facet	Ana S. Ramírez Jérémy Boilevin Ahmad Reza Mehdipour Gerhard Hummer Tamis Darbre Jean-Louis Reymond Kaspar P. Locher
author_sort	Ana S. Ramírez
title	Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
title_short	Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
title_full	Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
title_fullStr	Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
title_full_unstemmed	Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
title_sort	structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/02fd06bf76d44363ac10479a0e87396b
work_keys_str_mv	AT anasramirez structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT jeremyboilevin structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT ahmadrezamehdipour structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT gerhardhummer structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT tamisdarbre structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT jeanlouisreymond structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase AT kasparplocher structuralbasisofthemolecularrulermechanismofabacterialglycosyltransferase
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Structural basis of the molecular ruler mechanism of a bacterial glycosyltransferase

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