2QVJ

Crystal structure of a vesicular stomatitis virus nucleocapsid protein Ser290Trp mutant

2QVJ の概要

• エントリーDOI: 10.2210/pdb2qvj/pdb
• 分子名称: Nucleocapsid protein (1 entity in total)
• 機能のキーワード: nucleocapsid, cytoplasm, ribonucleoprotein, rna-binding, viral nucleoprotein, virion, rna binding protein
• 由来する生物種: Vesicular stomatitis Indiana virus
• 細胞内の位置: Virion: P03521
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 237159.42

構造登録者

Luo, M.,Green, T.J.,Zhang, X.,Tsao, J.,Qiu, S. (登録日: 2007-08-08, 公開日: 2008-01-08, 最終更新日: 2024-02-21)

主引用文献

Zhang, X.,Green, T.J.,Tsao, J.,Qiu, S.,Luo, M.
Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation.
J.Virol., 82:674-682, 2008

PubMed Abstract: The crystal structure of the vesicular stomatitis virus nucleoprotein (N) in complex with RNA reveals extensive and specific intermolecular interactions among the N molecules in the 10-member oligomer. What roles these interactions play in encapsidating RNA was studied by mutagenesis of the N protein. Three N mutants intended for disruption of the intermolecular interactions were designed and coexpressed with the phosphoprotein (P) in an Escherichia coli system previously described (T. J. Green et al., J. Virol. 74:9515-9524, 2000). Mutants N (Delta1-22), N (Delta347-352), and N (320-324, (Ala)(5)) lost RNA encapsidation and oligomerization but still bound with P. Another mutant, N (Ser290-->Trp), was able to form a stable ring-like N oligomer and bind with the P protein but was no longer able to encapsidate RNA. The crystal structure of N (Ser290-->Trp) at 2.8 A resolution showed that this mutant can maintain all the same intermolecular interactions as the wild-type N except for a slight unwinding of the N-terminal lobe. These results suggest that the intermolecular contacts among the N molecules are required for encapsidation of the viral RNA.

PubMed: 18003727
DOI: 10.1128/JVI.00935-07

実験手法

X-RAY DIFFRACTION (2.8 Å)