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

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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Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2021-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-021-22093-4
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spelling doaj-1e9f084757d3479aa82cffe48fcd91582021-03-28T11:13:09ZengNature Publishing GroupNature Communications2041-17232021-03-0112111110.1038/s41467-021-22093-4The actomyosin interface contains an evolutionary conserved core and an ancillary interface involved in specificityJulien Robert-Paganin0Xiao-Ping Xu1Mark F. Swift2Daniel Auguin3James P. Robblee4Hailong Lu5Patricia M. Fagnant6Elena B. Krementsova7Kathleen M. Trybus8Anne Houdusse9Niels Volkmann10Dorit Hanein11Structural Motility, Institut Curie, CNRS, UMR 144Scintillon InstituteScintillon InstituteStructural Motility, Institut Curie, CNRS, UMR 144Department of Molecular Physiology & Biophysics, University of VermontDepartment of Molecular Physiology & Biophysics, University of VermontDepartment of Molecular Physiology & Biophysics, University of VermontDepartment of Molecular Physiology & Biophysics, University of VermontDepartment of Molecular Physiology & Biophysics, University of VermontStructural Motility, Institut Curie, CNRS, UMR 144Scintillon InstituteScintillon InstitutePlasmodium 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.https://doi.org/10.1038/s41467-021-22093-4
collection DOAJ
language English
format Article
sources DOAJ
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
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2021-03-01
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.
url https://doi.org/10.1038/s41467-021-22093-4
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