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dc.contributor.authorSarker, Subir
dc.contributor.authorTerron-Orellana, Maria Carmen 
dc.contributor.authorKhandokar, Yogesh
dc.contributor.authorAragão, David
dc.contributor.authorHardy, Joshua M
dc.contributor.authorRadjainia, Mazdak
dc.contributor.authorJiménez-Zaragoza, Manuel
dc.contributor.authorde Pablo, Pedro J
dc.contributor.authorCoulibaly, Fasséli
dc.contributor.authorLuque, Daniel 
dc.contributor.authorRaidal, Shane R
dc.contributor.authorForwood, Jade K
dc.date.accessioned2020-03-18T07:49:30Z
dc.date.available2020-03-18T07:49:30Z
dc.date.issued2016
dc.identifier.citationNat Commun. 2016 Oct 4;7:13014.es_ES
dc.identifier.issn2041-1723es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/9267
dc.description.abstractThe assembly and regulation of viral capsid proteins into highly ordered macromolecular complexes is essential for viral replication. Here, we utilize crystal structures of the capsid protein from the smallest and simplest known viruses capable of autonomously replicating in animal cells, circoviruses, to establish structural and mechanistic insights into capsid morphogenesis and regulation. The beak and feather disease virus, like many circoviruses, encode only two genes: a capsid protein and a replication initiation protein. The capsid protein forms distinct macromolecular assemblies during replication and here we elucidate these structures at high resolution, showing that these complexes reverse the exposure of the N-terminal arginine rich domain responsible for DNA binding and nuclear localization. We show that assembly of these complexes is regulated by single-stranded DNA (ssDNA), and provide a structural basis of capsid assembly around single-stranded DNA, highlighting novel binding interfaces distinct from the highly positively charged N-terminal ARM domain.es_ES
dc.description.sponsorshipJ.K.F. and F.C. are funded by Future Fellowships of the Australian Research Council. We thank the Clive and Vera Ramaciotti Centre for Cryo Electron Microscopy and the Australian Synchrotron for their technical support.es_ES
dc.language.isoenges_ES
dc.publisherNature Researches_ES
dc.relation.isversionofPublisher's versiones_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subject.meshAnimals es_ES
dc.subject.meshArginine es_ES
dc.subject.meshCapsid es_ES
dc.subject.meshCapsid Proteins es_ES
dc.subject.meshCrystallography, X-Ray es_ES
dc.subject.meshDNA Replication es_ES
dc.subject.meshDNA, Single-Stranded es_ES
dc.subject.meshDNA, Viral es_ES
dc.subject.meshMacromolecular Substances es_ES
dc.subject.meshProtein Conformation es_ES
dc.subject.meshProtein Domains es_ES
dc.subject.meshVirion es_ES
dc.subject.meshVirus Assembly es_ES
dc.subject.meshVirus Replication es_ES
dc.titleStructural insights into the assembly and regulation of distinct viral capsid complexeses_ES
dc.typeArtículoes_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID27698405es_ES
dc.format.volume7es_ES
dc.format.number1es_ES
dc.format.page13014es_ES
dc.identifier.doi10.1038/ncomms13014es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn2041-1723es_ES
dc.relation.publisherversionhttps://doi.org/10.1038/ncomms13014es_ES
dc.identifier.journalNature communicationses_ES
dc.repisalud.centroISCIII::Centro Nacional de Microbiologíaes_ES
dc.repisalud.institucionISCIIIes_ES
dc.rights.accessRightsinfo:eu-repo/semantics/openAccesses_ES


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Atribución 4.0 Internacional
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