8B8V

Crystal structure of the Rabies virus RNA free nucleoprotein- phosphoprotein complex

8B8V の概要

• エントリーDOI: 10.2210/pdb8b8v/pdb
• 分子名称: Nucleoprotein, Phosphoprotein, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: chaperone, complex, replication machinery, virus, viral protein
• 由来する生物種: Lyssavirus rabies; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56817.80

構造登録者

Gerard, F.C.A.,Jamin, M.,Bourhis, J.M. (登録日: 2022-10-05, 公開日: 2023-03-15, 最終更新日: 2024-02-07)

主引用文献

Gerard, F.C.A.,Bourhis, J.M.,Mas, C.,Branchard, A.,Vu, D.D.,Varhoshkova, S.,Leyrat, C.,Jamin, M.
Structure and Dynamics of the Unassembled Nucleoprotein of Rabies Virus in Complex with Its Phosphoprotein Chaperone Module.
Viruses, 14:-, 2022

PubMed Abstract: As for all non-segmented negative RNA viruses, rabies virus has its genome packaged in a linear assembly of nucleoprotein (N), named nucleocapsid. The formation of new nucleocapsids during virus replication in cells requires the production of soluble N protein in complex with its phosphoprotein (P) chaperone. In this study, we reconstituted a soluble heterodimeric complex between an armless N protein of rabies virus (RABV), lacking its N-terminal subdomain (N), and a peptide encompassing the N chaperon module of the P protein. We showed that the chaperone module undergoes a disordered-order transition when it assembles with N and measured an affinity in the low nanomolar range using a competition assay. We solved the crystal structure of the complex at a resolution of 2.3 Å, unveiling the details of the conserved interfaces. MD simulations showed that both the chaperon module of P and RNA-mediated polymerization reduced the ability of the RNA binding cavity to open and close. Finally, by reconstituting a complex with full-length P protein, we demonstrated that each P dimer could independently chaperon two N molecules.

PubMed: 36560817
DOI: 10.3390/v14122813

実験手法

X-RAY DIFFRACTION (2.3 Å)