Structural basis of Naa20 activity towards a canonical NatB substrate

Layer et al. present a crystal structure of Naa20, the catalytic subunit of an N-terminal acetyltransferase NatB, in complex with its competitive inhibitor CoA-Ac-MDEL. They find that Naa20 alone can acetylate NatB in vitro while Naa25, the auxiliary subunit of Naa20, increases the substrate affinit...

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Autores principales:	Dominik Layer, Jürgen Kopp, Miriam Fontanillo, Maja Köhn, Karine Lapouge, Irmgard Sinning
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/a463882788334edf964135dfeb200861
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spelling	oai:doaj.org-article:a463882788334edf964135dfeb2008612021-12-02T11:45:59ZStructural basis of Naa20 activity towards a canonical NatB substrate10.1038/s42003-020-01546-42399-3642https://doaj.org/article/a463882788334edf964135dfeb2008612021-01-01T00:00:00Zhttps://doi.org/10.1038/s42003-020-01546-4https://doaj.org/toc/2399-3642Layer et al. present a crystal structure of Naa20, the catalytic subunit of an N-terminal acetyltransferase NatB, in complex with its competitive inhibitor CoA-Ac-MDEL. They find that Naa20 alone can acetylate NatB in vitro while Naa25, the auxiliary subunit of Naa20, increases the substrate affinity of Naa20. This study provides insights into the development of NAT inhibitors.Dominik LayerJürgen KoppMiriam FontanilloMaja KöhnKarine LapougeIrmgard SinningNature PortfolioarticleBiology (General)QH301-705.5ENCommunications Biology, Vol 4, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Biology (General) QH301-705.5
spellingShingle	Biology (General) QH301-705.5 Dominik Layer Jürgen Kopp Miriam Fontanillo Maja Köhn Karine Lapouge Irmgard Sinning Structural basis of Naa20 activity towards a canonical NatB substrate
description	Layer et al. present a crystal structure of Naa20, the catalytic subunit of an N-terminal acetyltransferase NatB, in complex with its competitive inhibitor CoA-Ac-MDEL. They find that Naa20 alone can acetylate NatB in vitro while Naa25, the auxiliary subunit of Naa20, increases the substrate affinity of Naa20. This study provides insights into the development of NAT inhibitors.
format	article
author	Dominik Layer Jürgen Kopp Miriam Fontanillo Maja Köhn Karine Lapouge Irmgard Sinning
author_facet	Dominik Layer Jürgen Kopp Miriam Fontanillo Maja Köhn Karine Lapouge Irmgard Sinning
author_sort	Dominik Layer
title	Structural basis of Naa20 activity towards a canonical NatB substrate
title_short	Structural basis of Naa20 activity towards a canonical NatB substrate
title_full	Structural basis of Naa20 activity towards a canonical NatB substrate
title_fullStr	Structural basis of Naa20 activity towards a canonical NatB substrate
title_full_unstemmed	Structural basis of Naa20 activity towards a canonical NatB substrate
title_sort	structural basis of naa20 activity towards a canonical natb substrate
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/a463882788334edf964135dfeb200861
work_keys_str_mv	AT dominiklayer structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate AT jurgenkopp structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate AT miriamfontanillo structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate AT majakohn structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate AT karinelapouge structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate AT irmgardsinning structuralbasisofnaa20activitytowardsacanonicalnatbsubstrate
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Structural basis of Naa20 activity towards a canonical NatB substrate

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