8IZL

Structure of the Mumps Virus L Protein Bound by Phosphoprotein Tetramer

Summary for 8IZL

• Entry DOI: 10.2210/pdb8izl/pdb
• EMDB information: 35864
• Descriptor: Phosphoprotein, RNA-directed RNA polymerase L, ZINC ION (3 entities in total)
• Functional Keywords: mumps virus polymerase complex, rna-dependent rna synthesis, large protein, phosphoprotein., viral protein
• Biological source: Mumps orthorubulavirus; More
• Total number of polymer chains: 5
• Total formula weight: 423568.18

Authors

Li, T.H.,Shen, Q.T. (deposition date: 2023-04-07, release date: 2024-04-17, Last modification date: 2024-06-05)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (2.93 Å)