4IDX
hexameric crystal structure of Schmallenberg virus nucleoprotein
Summary for 4IDX
Entry DOI | 10.2210/pdb4idx/pdb |
Related | 4IDU |
Descriptor | Nucleocapsid protein (2 entities in total) |
Functional Keywords | nucleoprotein, protects genomic rna, rna replication and transcription, sbv nucleoprotein, dna binding protein |
Biological source | Schmallenberg virus (SBV) |
Total number of polymer chains | 3 |
Total formula weight | 78624.87 |
Authors | |
Primary citation | Dong, 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: 23468499DOI: 10.1128/JVI.00223-13 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.21 Å) |
Structure validation
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