5T3T

Ebola virus VP30 CTD bound to nucleoprotein

5T3T の概要

• エントリーDOI: 10.2210/pdb5t3t/pdb
• 関連するPDBエントリー: 5T3W
• 分子名称: Fusion protein of Nucleoprotein and Minor nucleoprotein VP30, SULFATE ION (3 entities in total)
• 機能のキーワード: transcription, replication, regulator, co-factor, viral protein
• 由来する生物種: Zaire ebolavirus (strain Mayinga-76) (ZEBOV); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 220889.34

構造登録者

Kirchdoerfer, R.N.,Moyer, C.L.,Abelson, D.M.,Saphire, E.O. (登録日: 2016-08-26, 公開日: 2016-09-28, 最終更新日: 2023-10-04)

主引用文献

Kirchdoerfer, R.N.,Moyer, C.L.,Abelson, D.M.,Saphire, E.O.
The Ebola Virus VP30-NP Interaction Is a Regulator of Viral RNA Synthesis.
Plos Pathog., 12:e1005937-e1005937, 2016

PubMed Abstract: Filoviruses are capable of causing deadly hemorrhagic fevers. All nonsegmented negative-sense RNA-virus nucleocapsids are composed of a nucleoprotein (NP), a phosphoprotein (VP35) and a polymerase (L). However, the VP30 RNA-synthesis co-factor is unique to the filoviruses. The assembly, structure, and function of the filovirus RNA replication complex remain unclear. Here, we have characterized the interactions of Ebola, Sudan and Marburg virus VP30 with NP using in vitro biochemistry, structural biology and cell-based mini-replicon assays. We have found that the VP30 C-terminal domain interacts with a short peptide in the C-terminal region of NP. Further, we have solved crystal structures of the VP30-NP complex for both Ebola and Marburg viruses. These structures reveal that a conserved, proline-rich NP peptide binds a shallow hydrophobic cleft on the VP30 C-terminal domain. Structure-guided Ebola virus VP30 mutants have altered affinities for the NP peptide. Correlation of these VP30-NP affinities with the activity for each of these mutants in a cell-based mini-replicon assay suggests that the VP30-NP interaction plays both essential and inhibitory roles in Ebola virus RNA synthesis.

PubMed: 27755595
DOI: 10.1371/journal.ppat.1005937

実験手法

X-RAY DIFFRACTION (2.2 Å)