4IDX

hexameric crystal structure of Schmallenberg virus nucleoprotein

4IDX の概要

• エントリーDOI: 10.2210/pdb4idx/pdb
• 関連するPDBエントリー: 4IDU
• 分子名称: Nucleocapsid protein (2 entities in total)
• 機能のキーワード: nucleoprotein, protects genomic rna, rna replication and transcription, sbv nucleoprotein, dna binding protein
• 由来する生物種: Schmallenberg virus (SBV)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 78624.87

構造登録者

Dong, H.,Dong, C. (登録日: 2012-12-13, 公開日: 2013-04-24, 最終更新日: 2023-11-08)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (3.21 Å)