3PU1

Crystal Structure of a vesicular stomatitis virus nucleocapsid-polyG complex

3PU1 の概要

• エントリーDOI: 10.2210/pdb3pu1/pdb
• 関連するPDBエントリー: 3PTO 3PTX 3PU0 3PU4
• 分子名称: Nucleoprotein, RNA (45-MER), URANYL (VI) ION (3 entities in total)
• 機能のキーワード: rna, nucleocapsid, viral protein-rna complex, viral protein/rna
• 由来する生物種: Vesicular stomatitis Indiana virus (VSIV); 詳細
• 細胞内の位置: Virion : P03521
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 257553.61

構造登録者

Luo, M.,Green, T.J.,Rowse, M. (登録日: 2010-12-03, 公開日: 2011-01-12, 最終更新日: 2024-02-21)

主引用文献

Green, T.J.,Rowse, M.,Tsao, J.,Kang, J.,Ge, P.,Zhou, Z.H.,Luo, M.
Access to RNA Encapsidated in the Nucleocapsid of Vesicular Stomatitis Virus.
J.Virol., 85:2714-2722, 2011

PubMed Abstract: The genomic RNA of negative-strand RNA viruses, such as vesicular stomatitis virus (VSV), is completely enwrapped by the nucleocapsid protein (N) in every stage of virus infection. During viral transcription/replication, however, the genomic RNA in the nucleocapsid must be accessible by the virus-encoded RNA-dependent RNA polymerase in order to serve as the template for RNA synthesis. With the VSV nucleocapsid and a nucleocapsid-like particle (NLP) produced in Escherichia coli, we have found that the RNA in the VSV nucleocapsid can be removed by RNase A, in contrast to what was previously reported. Removal of the RNA did not disrupt the assembly of the N protein, resulting in an empty capsid. Polyribonucleotides were reencapsidated into the empty NLP, and the crystal structures were determined. The crystal structures revealed variable degrees of association of the N protein with a specific RNA sequence.

PubMed: 21177817
DOI: 10.1128/JVI.01927-10

実験手法

X-RAY DIFFRACTION (3.14 Å)