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dc.contributor.authorJenni, Simon
dc.contributor.authorBloyet, Louis-Marie
dc.contributor.authorDiaz-Avalos, Ruben
dc.contributor.authorLiang, Bo
dc.contributor.authorWhelan, Sean P.J.
dc.contributor.authorGrigorieff, Nikolaus
dc.contributor.authorHarrison, Stephen C.
dc.date2022-08-11T08:09:55.000
dc.date.accessioned2022-08-23T16:48:45Z
dc.date.available2022-08-23T16:48:45Z
dc.date.issued2020-01-07
dc.date.submitted2020-02-18
dc.identifier.citation<p>Jenni S, Bloyet LM, Diaz-Avalos R, Liang B, Whelan SPJ, Grigorieff N, Harrison SC. Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor. Cell Rep. 2020 Jan 7;30(1):53-60.e5. doi: 10.1016/j.celrep.2019.12.024. PMID: 31914397. <a href="https://doi.org/10.1016/j.celrep.2019.12.024">Link to article on publisher's site</a></p>
dc.identifier.issn2211-1247 (Electronic)
dc.identifier.doi10.1016/j.celrep.2019.12.024
dc.identifier.pmid31914397
dc.identifier.urihttp://hdl.handle.net/20.500.14038/41326
dc.description.abstractThe large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 A resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5' nucleotide.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=31914397&dopt=Abstract">Link to Article in PubMed</a></p>
dc.rightsCopyright 2019 The Authors. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectantiviral
dc.subjectebola
dc.subjectpolymerase
dc.subjectrabies
dc.subjectrespiratory syncytial virus
dc.subjectrhabdoviruses
dc.subjectAmino Acids, Peptides, and Proteins
dc.subjectBiochemistry, Biophysics, and Structural Biology
dc.subjectEnzymes and Coenzymes
dc.subjectNucleic Acids, Nucleotides, and Nucleosides
dc.subjectVirology
dc.subjectVirus Diseases
dc.subjectViruses
dc.titleStructure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor
dc.typeJournal Article
dc.source.journaltitleCell reports
dc.source.volume30
dc.source.issue1
dc.identifier.legacyfulltexthttps://escholarship.umassmed.edu/cgi/viewcontent.cgi?article=5129&amp;context=oapubs&amp;unstamped=1
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/oapubs/4110
dc.identifier.contextkey16574422
refterms.dateFOA2022-08-23T16:48:45Z
html.description.abstract<p>The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 A resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5' nucleotide.</p>
dc.identifier.submissionpathoapubs/4110
dc.contributor.departmentRNA Therapeutics Institute
dc.source.pages53-60.e5


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Copyright 2019 The Authors. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
Except where otherwise noted, this item's license is described as Copyright 2019 The Authors. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).