9CGI

Cryo-EM structure of the Nipah Virus polymerase (L) protein in complex with the tetrameric phosphoprotein (P)

9CGI の概要

• エントリーDOI: 10.2210/pdb9cgi/pdb
• EMDBエントリー: 45580
• 分子名称: RNA-directed RNA polymerase L, Phosphoprotein (2 entities in total)
• 機能のキーワード: nipah virus, l protein, phosphoprotein, rna-dependent rna polymerase, prntase, gdp polyribonucleotidyl transferase, rna capping, viral replication, transferase, viral protein
• 由来する生物種: Henipavirus nipahense; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 571126.44

構造登録者

Liu, B.,Yang, G.,Wang, D. (登録日: 2024-06-29, 公開日: 2024-09-18, 最終更新日: 2024-10-23)

主引用文献

Yang, G.,Wang, D.,Liu, B.
Structure of the Nipah virus polymerase phosphoprotein complex.
Nat Commun, 15:8673-8673, 2024

PubMed Abstract: The Nipah virus (NiV), a member of the Paramyxoviridae family, is notorious for its high fatality rate in humans. The RNA polymerase machinery of NiV, comprising the large protein L and the phosphoprotein P, is essential for viral replication. This study presents the 2.9-Å cryo-electron microscopy structure of the NiV L-P complex, shedding light on its assembly and functionality. The structure not only demonstrates the molecular details of the conserved N-terminal domain, RNA-dependent RNA polymerase (RdRp), and GDP polyribonucleotidyltransferase of the L protein, but also the intact central oligomerization domain and the C-terminal X domain of the P protein. The P protein interacts extensively with the L protein, forming an antiparallel β-sheet among the P protomers and with the fingers subdomain of RdRp. The flexible linker domain of one P promoter extends its contact with the fingers subdomain to reach near the nascent RNA exit, highlighting the distinct characteristic of the NiV L-P interface. This distinctive tetrameric organization of the P protein and its interaction with the L protein provide crucial molecular insights into the replication and transcription mechanisms of NiV polymerase, ultimately contributing to the development of effective treatments and preventive measures against this Paramyxoviridae family deadly pathogen.

PubMed: 39375338
DOI: 10.1038/s41467-024-52701-y

実験手法

ELECTRON MICROSCOPY (2.92 Å)