6U1X

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

6U1X の概要

• エントリーDOI: 10.2210/pdb6u1x/pdb
• EMDBエントリー: 20614
• 分子名称: RNA-directed RNA polymerase L, Phosphoprotein, ZINC ION (3 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Vesicular stomatitis Indiana virus (strain San Juan) (VSIV); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 271386.66

構造登録者

Jenni, S.,Bloyet, L.M.,Dias-Avalos, R.,Liang, B.,Wheelman, S.P.J.,Grigorieff, N.,Harrison, S.C. (登録日: 2019-08-17, 公開日: 2020-01-22, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

ELECTRON MICROSCOPY (3 Å)