6U1X

Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor (3.0 A resolution)

Summary for 6U1X

• Entry DOI: 10.2210/pdb6u1x/pdb
• EMDB information: 20614
• Descriptor: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
• Functional Keywords: vesicular stomatitis virus, rna-dependent rna polymerase, l protein, p protein, phosphoprotein, single particle analysis, transcription, replication, virus, viral, rdrp, prntase, nonsegmented negative-sense rna viruses, viral protein
• Biological source: Vesicular stomatitis Indiana virus (strain San Juan) (VSIV); More
• Total number of polymer chains: 2
• Total formula weight: 271386.66

Authors

Jenni, S.,Bloyet, L.M.,Dias-Avalos, R.,Liang, B.,Wheelman, S.P.J.,Grigorieff, N.,Harrison, S.C. (deposition date: 2019-08-17, release date: 2020-01-22, Last modification date: 2024-03-20)

Primary citation

Jenni, S.,Bloyet, L.M.,Diaz-Avalos, R.,Liang, B.,Whelan, S.P.J.,Grigorieff, N.,Harrison, S.C.
Structure of the Vesicular Stomatitis Virus L Protein in Complex with Its Phosphoprotein Cofactor.
Cell Rep, 30:53-60.e5, 2020

PubMed Abstract: The large (L) proteins of non-segmented, negative-strand RNA viruses are multifunctional enzymes that produce capped, methylated, and polyadenylated mRNA and replicate the viral genome. A phosphoprotein (P), required for efficient RNA-dependent RNA polymerization from the viral ribonucleoprotein (RNP) template, regulates the function and conformation of the L protein. We report the structure of vesicular stomatitis virus L in complex with its P cofactor determined by electron cryomicroscopy at 3.0 Å resolution, enabling us to visualize bound segments of P. The contacts of three P segments with multiple L domains show how P induces a closed, compact, initiation-competent conformation. Binding of P to L positions its N-terminal domain adjacent to a putative RNA exit channel for efficient encapsidation of newly synthesized genomes with the nucleoprotein and orients its C-terminal domain to interact with an RNP template. The model shows that a conserved tryptophan in the priming loop can support the initiating 5' nucleotide.

PubMed: 31914397
DOI: 10.1016/j.celrep.2019.12.024

Experimental method

ELECTRON MICROSCOPY (3 Å)