8izl

Structure of the Mumps Virus L Protein Bound by Phosphoprotein Tetramer

spinqualitylabelsall models 8izl, resolution 2.93Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8izl is a 5 chain structure with sequence from Mumps orthorubulavirus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.93Å Ligands: ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q9J4L6_MUMPJ Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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