8X01

Structure of the Mumps Virus L Protein (state2) Bound by Phosphoprotein Tetramer

8X01 の概要

• エントリーDOI: 10.2210/pdb8x01/pdb
• EMDBエントリー: 37964
• 分子名称: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
• 機能のキーワード: mumps virus polymerase complex, rna-dependent rna synthesis, large protein, phosphoprotein., viral protein
• 由来する生物種: Mumps orthorubulavirus; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 423568.18

構造登録者

Li, T.H.,Shen, Q.T. (登録日: 2023-11-02, 公開日: 2024-06-05)

主引用文献

Li, T.,Liu, M.,Gu, Z.,Su, X.,Liu, Y.,Lin, J.,Zhang, Y.,Shen, Q.T.
Structures of the mumps virus polymerase complex via cryo-electron microscopy.
Nat Commun, 15:4189-4189, 2024

PubMed Abstract: The viral polymerase complex, comprising the large protein (L) and phosphoprotein (P), is crucial for both genome replication and transcription in non-segmented negative-strand RNA viruses (nsNSVs), while structures corresponding to these activities remain obscure. Here, we resolved two L-P complex conformations from the mumps virus (MuV), a typical member of nsNSVs, via cryogenic-electron microscopy. One conformation presents all five domains of L forming a continuous RNA tunnel to the methyltransferase domain (MTase), preferably as a transcription state. The other conformation has the appendage averaged out, which is inaccessible to MTase. In both conformations, parallel P tetramers are revealed around MuV L, which, together with structures of other nsNSVs, demonstrates the diverse origins of the L-binding X domain of P. Our study links varying structures of nsNSV polymerase complexes with genome replication and transcription and points to a sliding model for polymerase complexes to advance along the RNA templates.

PubMed: 38760379
DOI: 10.1038/s41467-024-48389-9

実験手法

ELECTRON MICROSCOPY (3.01 Å)