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- PDB-7nt5: CryoEM structure of the Nipah virus nucleocapsid single helical t... -
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Basic information
Entry | Database: PDB / ID: 7nt5 | ||||||
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Title | CryoEM structure of the Nipah virus nucleocapsid single helical turn assembly | ||||||
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![]() | VIRAL PROTEIN / Protein-RNA complex / Nucleocapsid | ||||||
Function / homology | ![]() negative stranded viral RNA transcription / negative stranded viral RNA replication / helical viral capsid / viral nucleocapsid / host cell cytoplasm / molecular adaptor activity / ribonucleoprotein complex / structural molecule activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
![]() | Ker, D.S. / Jenkins, H.T. / Greive, S.J. / Antson, A.A. | ||||||
Funding support | ![]()
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![]() | ![]() Title: CryoEM structure of the Nipah virus nucleocapsid assembly. Authors: De-Sheng Ker / Huw T Jenkins / Sandra J Greive / Alfred A Antson / ![]() Abstract: Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we ...Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus RNA-bound nucleocapsid assembly, at 3.5 Å resolution. The helical assembly is stabilised by previously undefined N- and C-terminal segments, contributing to subunit-subunit interactions. RNA is wrapped around the nucleocapsid protein assembly with a periodicity of six nucleotides per protomer, in the "3-bases-in, 3-bases-out" conformation, with protein plasticity enabling non-sequence specific interactions. The structure reveals commonalities in RNA binding pockets and in the conformation of bound RNA, not only with members of the Paramyxoviridae family, but also with the evolutionarily distant Filoviridae Ebola virus. Significant structural differences with other Paramyxoviridae members are also observed, particularly in the position and length of the exposed α-helix, residues 123-139, which may serve as a valuable epitope for surveillance and diagnostics. | ||||||
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Structure visualization
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-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 141.3 KB | Display | |
Data in CIF | ![]() | 219.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 12581MC ![]() 7nt6C M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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