High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation

N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive cognate lipid and peptide substrates and further s...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Cyril Dian, Inmaculada Pérez-Dorado, Frédéric Rivière, Thomas Asensio, Pierre Legrand, Markus Ritzefeld, Mengjie Shen, Ernesto Cota, Thierry Meinnel, Edward W. Tate, Carmela Giglione
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1d7d6b525886413db95bc8b3e99c1d00
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:1d7d6b525886413db95bc8b3e99c1d00
record_format	dspace
spelling	oai:doaj.org-article:1d7d6b525886413db95bc8b3e99c1d002021-12-02T14:42:28ZHigh-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation10.1038/s41467-020-14847-32041-1723https://doaj.org/article/1d7d6b525886413db95bc8b3e99c1d002020-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14847-3https://doaj.org/toc/2041-1723N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive cognate lipid and peptide substrates and further show that NMT1 also catalyses the acylation of N-terminal lysines.Cyril DianInmaculada Pérez-DoradoFrédéric RivièreThomas AsensioPierre LegrandMarkus RitzefeldMengjie ShenErnesto CotaThierry MeinnelEdward W. TateCarmela GiglioneNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Cyril Dian Inmaculada Pérez-Dorado Frédéric Rivière Thomas Asensio Pierre Legrand Markus Ritzefeld Mengjie Shen Ernesto Cota Thierry Meinnel Edward W. Tate Carmela Giglione High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
description	N-terminal glycine myristoyl transferases (NMTs) catalyse the myristoylation of eukaryotic proteins. Here, the authors provide insights into the catalytic mechanism of NMTs by determining the crystal structures of human NMT1 in complex with reactive cognate lipid and peptide substrates and further show that NMT1 also catalyses the acylation of N-terminal lysines.
format	article
author	Cyril Dian Inmaculada Pérez-Dorado Frédéric Rivière Thomas Asensio Pierre Legrand Markus Ritzefeld Mengjie Shen Ernesto Cota Thierry Meinnel Edward W. Tate Carmela Giglione
author_facet	Cyril Dian Inmaculada Pérez-Dorado Frédéric Rivière Thomas Asensio Pierre Legrand Markus Ritzefeld Mengjie Shen Ernesto Cota Thierry Meinnel Edward W. Tate Carmela Giglione
author_sort	Cyril Dian
title	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
title_short	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
title_full	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
title_fullStr	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
title_full_unstemmed	High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation
title_sort	high-resolution snapshots of human n-myristoyltransferase in action illuminate a mechanism promoting n-terminal lys and gly myristoylation
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/1d7d6b525886413db95bc8b3e99c1d00
work_keys_str_mv	AT cyrildian highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT inmaculadaperezdorado highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT fredericriviere highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT thomasasensio highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT pierrelegrand highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT markusritzefeld highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT mengjieshen highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT ernestocota highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT thierrymeinnel highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT edwardwtate highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation AT carmelagiglione highresolutionsnapshotsofhumannmyristoyltransferaseinactionilluminateamechanismpromotingnterminallysandglymyristoylation
_version_	1718389676324159488

High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation

Ejemplares similares