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dc.contributor.author
Turowski, Valeria Rosana
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dc.contributor.author
Ruiz, Diego Mario
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dc.contributor.author
Nascimento, Andrey F. Z.
dc.contributor.author
Millán, Claudia
dc.contributor.author
Sammito, Massimo D.
dc.contributor.author
Juanhuix, Judith
dc.contributor.author
Cremonesi, Aline Sampaio
dc.contributor.author
Usón, Isabel
dc.contributor.author
Giuseppea, Priscila O.
dc.contributor.author
Murakamia, Mario T.
dc.date.available
2022-08-11T13:37:48Z
dc.date.issued
2021-02
dc.identifier.citation
Turowski, Valeria Rosana; Ruiz, Diego Mario; Nascimento, Andrey F. Z.; Millán, Claudia; Sammito, Massimo D.; et al.; Structure of the class XI myosin globular tail reveals evolutionary hallmarks for cargo recognition in plants; Wiley Blackwell Publishing, Inc; Acta Crystallographica Section D-Biological Crystallography; 77; 2-2021; 522-533
dc.identifier.issn
0907-4449
dc.identifier.uri
http://hdl.handle.net/11336/165161
dc.description.abstract
The plant-specific class XI myosins (MyoXIs) play key roles at the molecular, cellular and tissue levels, engaging diverse adaptor proteins to transport cargoes along actin filaments. To recognize their cargoes, MyoXIs have a C-terminal globular tail domain (GTD) that is evolutionarily related to those of class V myosins (MyoVs) from animals and fungi. Despite recent advances in understanding the functional roles played by MyoXI in plants, the structure of its GTD, and therefore the molecular determinants for cargo selectivity and recognition, remain elusive. In this study, the first crystal structure of a MyoXI GTD, that of MyoXI-K from Arabidopsis thaliana, was elucidated at 2.35 Å resolution using a low-identity and fragment-based phasing approach in ARCIMBOLDO_SHREDDER. The results reveal that both the composition and the length of the α5- α6 loop are distinctive features of MyoXI-K, providing evidence for a structural stabilizing role for this loop, which is otherwise carried out by a molecular zipper in MyoV GTDs. The crystal structure also shows that most of the characterized cargo-binding sites in MyoVs are not conserved in plant MyoXIs, pointing to plant-specific cargo-recognition mechanisms. Notably, the main elements involved in the self-regulation mechanism of MyoVs are conserved in plant MyoXIs, indicating this to be an ancient ancestral trait.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
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dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
MEMBRANE TRAFFICKING
dc.subject
MOLECULAR MOTOR
dc.subject
CLASS XI MYOSIN
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GLOBULAR TAIL DOMAIN
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ARABIDOPSIS THALIANA
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CRYSTAL STRUCTURE
dc.subject
ARCIMBOLDO
dc.subject.classification
Biofísica
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Structure of the class XI myosin globular tail reveals evolutionary hallmarks for cargo recognition in plants
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2022-08-03T18:13:44Z
dc.journal.volume
77
dc.journal.pagination
522-533
dc.journal.pais
Reino Unido
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dc.journal.ciudad
Londres
dc.description.fil
Fil: Turowski, Valeria Rosana. Brazilian Center for Research in Energy and Materials; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Ruiz, Diego Mario. Brazilian Center for Research in Energy and Materials; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Universidad Nacional de San Martín. Instituto de Investigaciones Biotecnológicas; Argentina
dc.description.fil
Fil: Nascimento, Andrey F. Z.. Instituto de Biología Molecular de Barcelona; España. Consejo Superior de Investigaciones Científicas; España. ALBA Synchrotron Light Source; España. Brazilian Center for Research in Energy and Materials; Brasil
dc.description.fil
Fil: Millán, Claudia. Instituto de Biología Molecular de Barcelona; España. Consejo Superior de Investigaciones Científicas; España
dc.description.fil
Fil: Sammito, Massimo D.. University of Cambridge; Estados Unidos
dc.description.fil
Fil: Juanhuix, Judith. Alba Synchrotron Light Facility; Brasil
dc.description.fil
Fil: Cremonesi, Aline Sampaio. Brazilian Center for Research in Energy and Materials; Brasil. Universidade Sao Francisco; Brasil
dc.description.fil
Fil: Usón, Isabel. Instituto de Biología Molecular de Barcelona; España. Consejo Superior de Investigaciones Científicas; España. Institucio´ Catalana de Recerca i Estudis Avanc¸ats; España
dc.description.fil
Fil: Giuseppea, Priscila O.. Brazilian Center for Research in Energy and Materials; Brasil
dc.description.fil
Fil: Murakamia, Mario T.. Brazilian Center for Research in Energy and Materials; Brasil
dc.journal.title
Acta Crystallographica Section D-Biological Crystallography
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1107/S2059798321001583
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://scripts.iucr.org/cgi-bin/paper?S2059798321001583
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