The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity

Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and...

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Autores principales:	Julien Robert-Paganin, Xiao-Ping Xu, Mark F. Swift, Daniel Auguin, James P. Robblee, Hailong Lu, Patricia M. Fagnant, Elena B. Krementsova, Kathleen M. Trybus, Anne Houdusse, Niels Volkmann, Dorit Hanein
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/1e9f084757d3479aa82cffe48fcd9158
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spelling	oai:doaj.org-article:1e9f084757d3479aa82cffe48fcd91582021-12-02T17:04:01ZThe actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity10.1038/s41467-021-22093-42041-1723https://doaj.org/article/1e9f084757d3479aa82cffe48fcd91582021-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22093-4https://doaj.org/toc/2041-1723Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.Julien Robert-PaganinXiao-Ping XuMark F. SwiftDaniel AuguinJames P. RobbleeHailong LuPatricia M. FagnantElena B. KrementsovaKathleen M. TrybusAnne HoudusseNiels VolkmannDorit HaneinNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Julien Robert-Paganin Xiao-Ping Xu Mark F. Swift Daniel Auguin James P. Robblee Hailong Lu Patricia M. Fagnant Elena B. Krementsova Kathleen M. Trybus Anne Houdusse Niels Volkmann Dorit Hanein The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
description	Plasmodium falciparum moves by an atypical process called gliding motility which comprises of atypical myosin A (PfMyoA) and filaments of the dynamic and divergent PfActin-1 (PfAct1). Here authors present the cryo-EM structure of PfMyoA bound to filamentous PfAct1 stabilized with jasplakinolide and provide insights into the interactions that are required for the parasite to produce the force and motion required for infectivity.
format	article
author	Julien Robert-Paganin Xiao-Ping Xu Mark F. Swift Daniel Auguin James P. Robblee Hailong Lu Patricia M. Fagnant Elena B. Krementsova Kathleen M. Trybus Anne Houdusse Niels Volkmann Dorit Hanein
author_facet	Julien Robert-Paganin Xiao-Ping Xu Mark F. Swift Daniel Auguin James P. Robblee Hailong Lu Patricia M. Fagnant Elena B. Krementsova Kathleen M. Trybus Anne Houdusse Niels Volkmann Dorit Hanein
author_sort	Julien Robert-Paganin
title	The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
title_short	The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
title_full	The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
title_fullStr	The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
title_full_unstemmed	The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
title_sort	actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/1e9f084757d3479aa82cffe48fcd9158
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The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificity

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