Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates

The conserved eukaryotic heterotrimeric NatC complex co-translationally acetylates the N-termini of numerous target proteins. Here, the authors provide insights into the catalytic mechanism of NatC by determining the crystal structures of Saccharomyces cerevisiae NatC in the absence and presence of...

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Autores principales:	Stephan Grunwald, Linus V. M. Hopf, Tobias Bock-Bierbaum, Ciara C. M. Lally, Christian M. T. Spahn, Oliver Daumke
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/600264e4d8b44389bdb8c8442cd3c649
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spelling	oai:doaj.org-article:600264e4d8b44389bdb8c8442cd3c6492021-12-02T15:39:21ZDivergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates10.1038/s41467-020-19321-82041-1723https://doaj.org/article/600264e4d8b44389bdb8c8442cd3c6492020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19321-8https://doaj.org/toc/2041-1723The conserved eukaryotic heterotrimeric NatC complex co-translationally acetylates the N-termini of numerous target proteins. Here, the authors provide insights into the catalytic mechanism of NatC by determining the crystal structures of Saccharomyces cerevisiae NatC in the absence and presence of cofactors and peptide substrates and reveal the molecular basis of substrate binding by further biochemical analyses.Stephan GrunwaldLinus V. M. HopfTobias Bock-BierbaumCiara C. M. LallyChristian M. T. SpahnOliver DaumkeNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Stephan Grunwald Linus V. M. Hopf Tobias Bock-Bierbaum Ciara C. M. Lally Christian M. T. Spahn Oliver Daumke Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
description	The conserved eukaryotic heterotrimeric NatC complex co-translationally acetylates the N-termini of numerous target proteins. Here, the authors provide insights into the catalytic mechanism of NatC by determining the crystal structures of Saccharomyces cerevisiae NatC in the absence and presence of cofactors and peptide substrates and reveal the molecular basis of substrate binding by further biochemical analyses.
format	article
author	Stephan Grunwald Linus V. M. Hopf Tobias Bock-Bierbaum Ciara C. M. Lally Christian M. T. Spahn Oliver Daumke
author_facet	Stephan Grunwald Linus V. M. Hopf Tobias Bock-Bierbaum Ciara C. M. Lally Christian M. T. Spahn Oliver Daumke
author_sort	Stephan Grunwald
title	Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
title_short	Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
title_full	Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
title_fullStr	Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
title_full_unstemmed	Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates
title_sort	divergent architecture of the heterotrimeric natc complex explains n-terminal acetylation of cognate substrates
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/600264e4d8b44389bdb8c8442cd3c649
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Divergent architecture of the heterotrimeric NatC complex explains N-terminal acetylation of cognate substrates

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