7PNO

C terminal domain of Nipah Virus Phosphoprotein fused to the Ntail alpha more of the Nucleoprotein.

Summary for 7PNO

• Entry DOI: 10.2210/pdb7pno/pdb
• Descriptor: Phosphoprotein, alpha MoRE of Nipah virus Nucleoprotein tail (3 entities in total)
• Functional Keywords: nipah virus, phosphoprotein, viral protein, polymerase cofactor
• Biological source: Nipah virus; More
• Total number of polymer chains: 14
• Total formula weight: 71492.23

Authors

Bourhis, J.M.,Yabukaski, F.,Tarbouriech, N.,Jamin, M. (deposition date: 2021-09-07, release date: 2022-04-20, Last modification date: 2024-06-19)

Primary citation

Bourhis, J.M.,Yabukarski, F.,Communie, G.,Schneider, R.,Volchkova, V.A.,Freneat, M.,Gerard, F.C.,Ducournau, C.,Mas, C.,Tarbouriech, N.,Ringkjobing Jensen, M.,Volchkov, V.E.,Blackledge, M.,Jamin, M.
Structural Dynamics of the C-terminal X Domain of Nipah and Hendra Viruses Controls the Attachment to the C-terminal Tail of the Nucleocapsid Protein.
J.Mol.Biol., 434:167551-167551, 2022

PubMed Abstract: To understand the dynamic interactions between the phosphoprotein (P) and the nucleoprotein (N) within the transcription/replication complex of the Paramyxoviridae and to decipher their roles in regulating viral multiplication, we characterized the structural properties of the C-terminal X domain (P) of Nipah (NiV) and Hendra virus (HeV) P protein. In crystals, isolated NiV P adopted a two-helix dimeric conformation, which was incompetent for binding its partners, but in complex with the C-terminal intrinsically disordered tail of the N protein (N), it folded into a canonical 3H bundle conformation. In solution, SEC-MALLS, SAXS and NMR spectroscopy experiments indicated that both NiV and HeV P were larger in size than expected for compact proteins of the same molecular mass and were in conformational exchange between a compact three-helix (3H) bundle and partially unfolded conformations, where helix α is detached from the other two. Some measurements also provided strong evidence for dimerization of NiV P in solution but not for HeV P. Ensemble modeling of experimental SAXS data and statistical-dynamical modeling reconciled all these data, yielding a model where NiV and HeV P exchanged between different conformations, and where NiV but not HeV P formed dimers. Finally, recombinant NiV comprising a chimeric P carrying HeV P was rescued and compared with parental NiV. Experiments carried out in cellula demonstrated that the replacement of P did not significantly affect the replication dynamics while caused a slight virus attenuation, suggesting a possible role of the dimerization of NiV P in viral replication.

PubMed: 35317998
DOI: 10.1016/j.jmb.2022.167551

Experimental method

X-RAY DIFFRACTION (2.79 Å)