2I8B

Crystal structure of the C-terminal domain of Ebola virus VP30

2I8B の概要

• エントリーDOI: 10.2210/pdb2i8b/pdb
• 分子名称: Minor nucleoprotein VP30 (2 entities in total)
• 機能のキーワード: vp30 ebola virus protein, transcription, rna binding, viral protein
• 由来する生物種: Zaire ebolavirus
• 細胞内の位置: Virion: Q05323
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35071.14

構造登録者

Muziol, T.M.,Hartlieb, B.,Becker, S.,Weissenhorn, W. (登録日: 2006-09-01, 公開日: 2007-01-23, 最終更新日: 2024-10-09)

主引用文献

Hartlieb, B.,Muziol, T.,Weissenhorn, W.,Becker, S.
Crystal structure of the C-terminal domain of Ebola virus VP30 reveals a role in transcription and nucleocapsid association.
Proc.Natl.Acad.Sci.Usa, 104:624-629, 2007

PubMed Abstract: Transcription of the highly pathogenic Ebola virus depends on VP30, a nucleocapsid-associated Ebola virus-specific transcription factor. The transcription activator VP30 was shown to play an essential role in Ebola virus replication, most likely by stabilizing nascent mRNA. Here we present the crystal structure of the C-terminal domain (CTD) of VP30 (VP30(CTD)) at 2.0-A resolution. VP30(CTD) folds independently into a dimeric helical assembly. The VP30(CTD) dimers assemble into hexamers that are present in virions, by an oligomerization domain located in the N terminus of VP30. Mutagenesis of conserved charged amino acids on VP30(CTD) revealed that two regions, namely a basic cluster around Lys-180 and Glu-197, are required for nucleocapsid interaction. However, only mutagenesis of the basic cluster was shown to impair transcription activation, suggesting that both processes are regulated independently. The structure and the mutagenesis results reveal a potential pocket for small-molecule inhibitors that might prevent VP30 activity and thus virus propagation as it has been shown previously by peptides, which interfere with VP30 homooligomerization.

PubMed: 17202263
DOI: 10.1073/pnas.0606730104

実験手法

X-RAY DIFFRACTION (2 Å)