EMDB/PDB/SASBDBから引用されている文献のデータベース

キーワード
構造解析手法	All X線回折 NMR 電子顕微鏡小角散乱中性子線回折線維回折粉末回折赤外分光 EPR FRET 理論モデルハイブリッド
著者・登録者
ジャーナル
IF	>30 >20 >10 >5 all

タイトル	Capping pores of alphavirus nsP1 gate membranous viral replication factories.
ジャーナル・号・ページ	Nature, Vol. 589, Issue 7843, Page 615-619, Year 2021
掲載日	2020年12月16日
著者	Rhian Jones / Gabriel Bragagnolo / Rocío Arranz / Juan Reguera /
PubMed 要旨	Positive-sense single-stranded RNA viruses, such as coronaviruses, flaviviruses and alphaviruses, carry out transcription and replication inside virus-induced membranous organelles within host cells. ...Positive-sense single-stranded RNA viruses, such as coronaviruses, flaviviruses and alphaviruses, carry out transcription and replication inside virus-induced membranous organelles within host cells. The remodelling of the host-cell membranes for the formation of these organelles is coupled to the membrane association of viral replication complexes and to RNA synthesis. These viral niches allow for the concentration of metabolites and proteins for the synthesis of viral RNA, and prevent the detection of this RNA by the cellular innate immune system. Here we present the cryo-electron microscopy structure of non-structural protein 1 (nsP1) of the alphavirus chikungunya virus, which is responsible for RNA capping and membrane binding of the viral replication machinery. The structure shows the enzyme in its active form, assembled in a monotopic membrane-associated dodecameric ring. The structure reveals the structural basis of the coupling between membrane binding, oligomerization and allosteric activation of the capping enzyme. The stoichiometry-with 12 active sites in a single complex-redefines viral replication complexes as RNA synthesis reactors. The ring shape of the complex implies it has a role in controlling access to the viral organelle and ensuring the exit of properly capped viral RNA. Our results provide high-resolution information about the membrane association of the replication machinery of positive-sense single-stranded RNA viruses, and open up avenues for the further characterization of viral replication on cell membranes and the generation of antiviral agents.
リンク	Nature / PubMed:33328629 / PubMed Central
手法	EM (単粒子)
解像度	2.6 - 2.9 Å
構造データ	11023 6z0u EMDB-11023, PDB-6z0u: CryoEM structure of the Chikungunya virus nsP1 complex 手法: EM (単粒子) / 解像度: 2.9 Å 11024 6z0v EMDB-11024, PDB-6z0v: CryoEM structure of the Chikungunya virus nsP1 complex 手法: EM (単粒子) / 解像度: 2.6 Å
化合物	ChemComp-ZN: Unknown entry ChemComp-HOH: WATER
由来	chikungunya virus strain s27-african prototype (ウイルス)
キーワード	VIRAL PROTEIN / Capping enzyme / monotopic membrane complex / membrane bending / membrane pore / replication complex / scaffold / Spherule formation / viral factory.