8FFR

Revised structure of the rabies virus nucleoprotein-RNA complex

8FFR の概要

• エントリーDOI: 10.2210/pdb8ffr/pdb
• 関連するPDBエントリー: 2gtt
• 分子名称: Nucleoprotein, RNA (99-MER), PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: protein-rna complex, rabies virus, nucleoprotein, viral protein, rna binding protein
• 由来する生物種: Rabies virus CVS-11; 詳細
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 1176436.18

構造登録者

Leyrat, C.,Bourhis, J.M.,Albertini, A.A.V.,Wernimont, A.K.,Muziol, T.,Ravelli, R.B.G.,Weissenhorn, W.,Ruigrok, R.W.H.,Jamin, M. (登録日: 2022-12-09, 公開日: 2023-01-11, 最終更新日: 2023-09-06)

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 (3.49 Å)