3PMK

Crystal structure of the Vesicular Stomatitis Virus RNA free nucleoprotein/phosphoprotein complex

3PMK の概要

• エントリーDOI: 10.2210/pdb3pmk/pdb
• 関連するPDBエントリー: 2GIC
• 分子名称: Nucleocapsid protein, Phosphoprotein (3 entities in total)
• 機能のキーワード: chaperone, viral protein
• 由来する生物種: Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 267485.78

構造登録者

Leyrat, C.,Yabukarski, F.,Tarbouriech, N.,Ruigrok, R.W.H.,Jamin, M. (登録日: 2010-11-17, 公開日: 2011-10-05, 最終更新日: 2023-09-06)

主引用文献

Leyrat, C.,Yabukarski, F.,Tarbouriech, N.,Ribeiro, E.A.,Jensen, M.R.,Blackledge, M.,Ruigrok, R.W.,Jamin, M.
Structure of the Vesicular Stomatitis Virus N0-P Complex
Plos Pathog., 7:e1002248-e1002248, 2011

PubMed Abstract: Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric complex between a variant of vesicular stomatitis virus N lacking its 21 N-terminal residues (N(Δ21)) and a peptide of 60 amino acids (P(60)) encompassing the molecular recognition element (MoRE) of P that binds RNA-free N (N(0)). The complex crystallized in a decameric circular form, which was solved at 3.0 Å resolution, reveals how the MoRE folds upon binding to N and competes with RNA binding and N polymerization. Small-angle X-ray scattering experiment and NMR spectroscopy on the soluble complex confirms the binding of the MoRE and indicates that its flanking regions remain flexible in the complex. The structure of this complex also suggests a mechanism for the initiation of viral RNA synthesis.

PubMed: 21960769
DOI: 10.1371/journal.ppat.1002248

実験手法

X-RAY DIFFRACTION (3.03 Å)