9FTF

Crystal structure of the Connecting Domain of the Nipah virus Large protein

9FTF の概要

• エントリーDOI: 10.2210/pdb9ftf/pdb
• 分子名称: RNA-directed RNA polymerase L, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: nipah virus l, connecting domain, viral protein
• 由来する生物種: Henipavirus nipahense
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 30890.52

構造登録者

Balikci, E.,Gunl, F.,Carrique, L.,Keown, J.R.,Fodor, E.,Grimes, J.M. (登録日: 2024-06-24, 公開日: 2025-01-08, 最終更新日: 2025-01-22)

主引用文献

Balikci, E.,Gunl, F.,Carrique, L.,Keown, J.R.,Fodor, E.,Grimes, J.M.
Structure of the Nipah virus polymerase complex.
Embo J., 44:563-586, 2025

PubMed Abstract: Nipah virus is a highly virulent zoonotic paramyxovirus causing severe respiratory and neurological disease. Despite its lethality, there is no approved treatment for Nipah virus infection. The viral polymerase complex, composed of the polymerase (L) and phosphoprotein (P), replicates and transcribes the viral RNA genome. Here, we describe structures of the Nipah virus L-P polymerase complex and the L-protein's Connecting Domain (CD). The cryo-electron microscopy L-P complex structure reveals the organization of the RNA-dependent RNA polymerase (RdRp) and polyribonucleotidyl transferase (PRNTase) domains of the L-protein, and shows how the P-protein, which forms a tetramer, interacts with the RdRp-domain of the L-protein. The crystal structure of the CD-domain alone reveals binding of three Mg ions. Modelling of this domain onto an AlphaFold 3 model of an RNA-L-P complex suggests a catalytic role for one Mg ion in mRNA capping. These findings offer insights into the structural details of the L-P polymerase complex and the molecular interactions between L-protein and P-protein, shedding light on the mechanisms of the replication machinery. This work will underpin efforts to develop antiviral drugs that target the polymerase complex of Nipah virus.

PubMed: 39739115
DOI: 10.1038/s44318-024-00321-z

実験手法

X-RAY DIFFRACTION (1.85 Å)