Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA

PatA is a membrane-associated acyltransferase that is essential for the biosynthesis of mycobacterial glycolipids. Here, Albesa-Jovéet al. describe structures of PatA from Mycobacterium smegmatisin complex with acyl donors and show that catalysis occurs by an unusual charge-relay mechanism.

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Autores principales:	David Albesa-Jové, Zuzana Svetlíková, Montse Tersa, Enea Sancho-Vaello, Ana Carreras-González, Pascal Bonnet, Pedro Arrasate, Ander Eguskiza, Shiva K. Angala, Javier O. Cifuente, Jana Korduláková, Mary Jackson, Katarína Mikušová, Marcelo E. Guerin
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/345eecca519f4563aed75b57f445943c
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spelling	oai:doaj.org-article:345eecca519f4563aed75b57f445943c2021-12-02T15:33:49ZStructural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA10.1038/ncomms109062041-1723https://doaj.org/article/345eecca519f4563aed75b57f445943c2016-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms10906https://doaj.org/toc/2041-1723PatA is a membrane-associated acyltransferase that is essential for the biosynthesis of mycobacterial glycolipids. Here, Albesa-Jovéet al. describe structures of PatA from Mycobacterium smegmatisin complex with acyl donors and show that catalysis occurs by an unusual charge-relay mechanism.David Albesa-JovéZuzana SvetlíkováMontse TersaEnea Sancho-VaelloAna Carreras-GonzálezPascal BonnetPedro ArrasateAnder EguskizaShiva K. AngalaJavier O. CifuenteJana KordulákováMary JacksonKatarína MikušováMarcelo E. GuerinNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q David Albesa-Jové Zuzana Svetlíková Montse Tersa Enea Sancho-Vaello Ana Carreras-González Pascal Bonnet Pedro Arrasate Ander Eguskiza Shiva K. Angala Javier O. Cifuente Jana Korduláková Mary Jackson Katarína Mikušová Marcelo E. Guerin Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
description	PatA is a membrane-associated acyltransferase that is essential for the biosynthesis of mycobacterial glycolipids. Here, Albesa-Jovéet al. describe structures of PatA from Mycobacterium smegmatisin complex with acyl donors and show that catalysis occurs by an unusual charge-relay mechanism.
format	article
author	David Albesa-Jové Zuzana Svetlíková Montse Tersa Enea Sancho-Vaello Ana Carreras-González Pascal Bonnet Pedro Arrasate Ander Eguskiza Shiva K. Angala Javier O. Cifuente Jana Korduláková Mary Jackson Katarína Mikušová Marcelo E. Guerin
author_facet	David Albesa-Jové Zuzana Svetlíková Montse Tersa Enea Sancho-Vaello Ana Carreras-González Pascal Bonnet Pedro Arrasate Ander Eguskiza Shiva K. Angala Javier O. Cifuente Jana Korduláková Mary Jackson Katarína Mikušová Marcelo E. Guerin
author_sort	David Albesa-Jové
title	Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
title_short	Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
title_full	Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
title_fullStr	Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
title_full_unstemmed	Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA
title_sort	structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase pata
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/345eecca519f4563aed75b57f445943c
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Structural basis for selective recognition of acyl chains by the membrane-associated acyltransferase PatA

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