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4CSF

Structural insights into Toscana virus RNA encapsidation

Summary for 4CSF
Entry DOI10.2210/pdb4csf/pdb
Related4CSG
DescriptorNUCLEOPROTEIN, RNA (5'-R(*UP*GP*UP*GP*UP*UP*UP*CP*UP)-3'), ... (5 entities in total)
Functional Keywordsviral protein-rna complex, viral protein, nucleocapsid, nucleoprotein, hexameric, infectious, viral protein/rna
Biological sourceTOSCANA VIRUS
More
Total number of polymer chains36
Total formula weight699159.15
Authors
Olal, D.,Daumke, O. (deposition date: 2014-03-07, release date: 2014-04-09, Last modification date: 2024-05-08)
Primary citationOlal, D.,Dick, A.,Woods, V.L.,Liu, T.,Li, S.,Devignot, S.,Weber, F.,Saphire, E.O.,Daumke, O.
Structural Insights Into RNA Encapsidation and Helical Assembly of the Toscana Virus Nucleoprotein.
Nucleic Acids Res., 42:6025-, 2014
Cited by
PubMed Abstract: Toscana virus is an emerging bunyavirus in Mediterranean Europe where it accounts for 80% of pediatric meningitis cases during the summer. The negative-strand ribonucleic acid (RNA) genome of the virus is wrapped around the virally encoded nucleoprotein N to form the ribonucleoprotein complex (RNP). We determined crystal structures of hexameric N alone (apo) and in complex with a nonameric single-stranded RNA. RNA is sequestered in a sequence-independent fashion in a deep groove inside the hexamer. At the junction between two adjacent copies of Ns, RNA binding induced an inter-subunit rotation, which opened the RNA-binding tunnel and created a new assembly interface at the outside of the hexamer. Based on these findings, we suggest a structural model for how binding of RNA to N promotes the formation of helical RNPs, which are a characteristic hallmark of many negative-strand RNA viruses.
PubMed: 24688060
DOI: 10.1093/NAR/GKU229
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.598 Å)
Structure validation

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