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4IDX

hexameric crystal structure of Schmallenberg virus nucleoprotein

Summary for 4IDX
Entry DOI10.2210/pdb4idx/pdb
Related4IDU
DescriptorNucleocapsid protein (2 entities in total)
Functional Keywordsnucleoprotein, protects genomic rna, rna replication and transcription, sbv nucleoprotein, dna binding protein
Biological sourceSchmallenberg virus (SBV)
Total number of polymer chains3
Total formula weight78624.87
Authors
Dong, H.,Dong, C. (deposition date: 2012-12-13, release date: 2013-04-24, Last modification date: 2023-11-08)
Primary citationDong, H.,Li, P.,Elliott, R.M.,Dong, C.
Structure of Schmallenberg orthobunyavirus nucleoprotein suggests a novel mechanism of genome encapsidation
J.Virol., 87:5593-5601, 2013
Cited by
PubMed Abstract: Schmallenberg virus (SBV), a newly emerged orthobunyavirus (family Bunyaviridae), has spread rapidly across Europe and has caused congenital abnormalities in the offspring of cattle, sheep, and goats. Like other orthobunyaviruses, SBV contains a tripartite negative-sense RNA genome that encodes four structural and two nonstructural proteins. The nucleoprotein (N) encapsidates the three viral genomic RNA segments and plays a crucial role in viral RNA transcription and replication. Here we report the crystal structure of the bacterially expressed SBV nucleoprotein to a 3.06-Å resolution. The protomer is composed of two domains (N-terminal and C-terminal domains) with flexible N-terminal and C-terminal arms. The N protein has a novel fold and forms a central positively charged cleft for genomic RNA binding. The nucleoprotein purified under native conditions forms a tetramer, while the nucleoprotein obtained following denaturation and refolding forms a hexamer. Our structural and functional analyses demonstrate that both N-terminal and C-terminal arms are involved in N-N interaction and oligomerization and play an essential role in viral RNA synthesis, suggesting a novel mechanism for viral RNA encapsidation and transcription.
PubMed: 23468499
DOI: 10.1128/JVI.00223-13
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.21 Å)
Structure validation

237992

數據於2025-06-25公開中

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