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4IDU

crystal structure of Schmallenberg virus nucleoprotein

Summary for 4IDU
Entry DOI10.2210/pdb4idu/pdb
DescriptorSBV nucleoprotein (2 entities in total)
Functional Keywordsschmallenberg virus, nucleoprotein, protect genome rna, replication and transcription, dna binding protein
Biological sourceSchmallenberg virus (SBV)
More
Cellular locationVirion: H2AM13 H2AM13
Total number of polymer chains4
Total formula weight104926.96
Authors
Dong, H.,Li, P.,Elliott, R.M.,Dong, C. (deposition date: 2012-12-13, release date: 2013-04-24, Last modification date: 2024-10-30)
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 (3.08 Å)
Structure validation

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