Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s

Kinesin-13s are microtubule depolymerases that lack motile activity. Here the authors present the cryo-EM structures of kinesin-13 microtubule complexes in different nucleotide bound states, which reveal how ATP hydrolysis is linked to conformational changes and propose a model for kinesin induced d...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Matthieu P.M.H. Benoit, Ana B. Asenjo, Hernando Sosa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/c060d539f3bb453bab56271b9db5aab9
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:c060d539f3bb453bab56271b9db5aab9
record_format	dspace
spelling	oai:doaj.org-article:c060d539f3bb453bab56271b9db5aab92021-12-02T15:34:00ZCryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s10.1038/s41467-018-04044-82041-1723https://doaj.org/article/c060d539f3bb453bab56271b9db5aab92018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04044-8https://doaj.org/toc/2041-1723Kinesin-13s are microtubule depolymerases that lack motile activity. Here the authors present the cryo-EM structures of kinesin-13 microtubule complexes in different nucleotide bound states, which reveal how ATP hydrolysis is linked to conformational changes and propose a model for kinesin induced depolymerisation.Matthieu P.M.H. BenoitAna B. AsenjoHernando SosaNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Matthieu P.M.H. Benoit Ana B. Asenjo Hernando Sosa Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
description	Kinesin-13s are microtubule depolymerases that lack motile activity. Here the authors present the cryo-EM structures of kinesin-13 microtubule complexes in different nucleotide bound states, which reveal how ATP hydrolysis is linked to conformational changes and propose a model for kinesin induced depolymerisation.
format	article
author	Matthieu P.M.H. Benoit Ana B. Asenjo Hernando Sosa
author_facet	Matthieu P.M.H. Benoit Ana B. Asenjo Hernando Sosa
author_sort	Matthieu P.M.H. Benoit
title	Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
title_short	Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
title_full	Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
title_fullStr	Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
title_full_unstemmed	Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s
title_sort	cryo-em reveals the structural basis of microtubule depolymerization by kinesin-13s
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/c060d539f3bb453bab56271b9db5aab9
work_keys_str_mv	AT matthieupmhbenoit cryoemrevealsthestructuralbasisofmicrotubuledepolymerizationbykinesin13s AT anabasenjo cryoemrevealsthestructuralbasisofmicrotubuledepolymerizationbykinesin13s AT hernandososa cryoemrevealsthestructuralbasisofmicrotubuledepolymerizationbykinesin13s
_version_	1718386988853231616

Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s

Ejemplares similares