6OJ3

In situ structure of rotavirus VP1 RNA-dependent RNA polymerase (TLP)

これはPDB形式変換不可エントリーです。

6OJ3 の概要

• エントリーDOI: 10.2210/pdb6oj3/pdb
• EMDBエントリー: 20086 20087 20088 20089
• 分子名称: Inner capsid protein VP2, RNA-directed RNA polymerase (2 entities in total)
• 機能のキーワード: rotavirus, rna-dependent rna polymerase, vp1, vp2, viral protein-transferase complex, viral protein/transferase
• 由来する生物種: Rotavirus A (strain RVA/Monkey/United States/RRV/1975/G3P5B[3]) (RV-A); 詳細
• タンパク質・核酸の鎖数: 11
• 化学式量合計: 1159536.22

構造登録者

Jenni, S.,Salgado, E.N.,Herrmann, T.,Li, Z.,Grant, T.,Grigorieff, N.,Trapani, S.,Estrozi, L.F.,Harrison, S.C. (登録日: 2019-04-10, 公開日: 2019-04-24, 最終更新日: 2024-03-20)

主引用文献

Jenni, S.,Salgado, E.N.,Herrmann, T.,Li, Z.,Grant, T.,Grigorieff, N.,Trapani, S.,Estrozi, L.F.,Harrison, S.C.
In situ Structure of Rotavirus VP1 RNA-Dependent RNA Polymerase.
J.Mol.Biol., 431:3124-3138, 2019

PubMed Abstract: Rotaviruses, like other non-enveloped, double-strand RNA viruses, package an RNA-dependent RNA polymerase (RdRp) with each duplex of their segmented genomes. Rotavirus cell entry results in loss of an outer protein layer and delivery into the cytosol of an intact, inner capsid particle (the "double-layer particle," or DLP). The RdRp, designated VP1, is active inside the DLP; each VP1 achieves many rounds of mRNA transcription from its associated genome segment. Previous work has shown that one VP1 molecule lies close to each 5-fold axis of the icosahedrally symmetric DLP, just beneath the inner surface of its protein shell, embedded in tightly packed RNA. We have determined a high-resolution structure for the rotavirus VP1 RdRp in situ, by local reconstruction of density around individual 5-fold positions. We have analyzed intact virions ("triple-layer particles"), non-transcribing DLPs and transcribing DLPs. Outer layer dissociation enables the DLP to synthesize RNA, in vitro as well as in vivo, but appears not to induce any detectable structural change in the RdRp. Addition of NTPs, Mg, and S-adenosylmethionine, which allows active transcription, results in conformational rearrangements, in both VP1 and the DLP capsid shell protein, that allow a transcript to exit the polymerase and the particle. The position of VP1 (among the five symmetrically related alternatives) at one vertex does not correlate with its position at other vertices. This stochastic distribution of site occupancies limits long-range order in the 11-segment, double-strand RNA genome.

PubMed: 31233764
DOI: 10.1016/j.jmb.2019.06.016

実験手法

ELECTRON MICROSCOPY (4.5 Å)