8X01
Structure of the Mumps Virus L Protein (state2) Bound by Phosphoprotein Tetramer
Summary for 8X01
| Entry DOI | 10.2210/pdb8x01/pdb |
| EMDB information | 37964 |
| Descriptor | RNA-directed RNA polymerase L, Phosphoprotein, 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 | |
| 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 Cited by 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: 38760379DOI: 10.1038/s41467-024-48389-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.01 Å) |
Structure validation
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