8yxo
From Proteopedia
Structure of Phosphoprotein tetramer from mumps virus
Structural highlights
FunctionPublication Abstract from PubMedThe 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. Structures of the mumps virus polymerase complex via cryo-electron microscopy.,Li T, Liu M, Gu Z, Su X, Liu Y, Lin J, Zhang Y, Shen QT Nat Commun. 2024 May 17;15(1):4189. doi: 10.1038/s41467-024-48389-9. PMID:38760379[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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