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	Uncoating of common cold virus is preceded by RNA switching as determined by X-ray and cryo-EM analyses of the subviral A-particle.
ジャーナル・号・ページ	Proc Natl Acad Sci U S A, Vol. 110, Issue 50, Page 20063-20068, Year 2013
掲載日	2013年12月10日
著者	Angela Pickl-Herk / Daniel Luque / Laia Vives-Adrián / Jordi Querol-Audí / Damià Garriga / Benes L Trus / Nuria Verdaguer / Dieter Blaas / José R Castón /
PubMed 要旨	During infection, viruses undergo conformational changes that lead to delivery of their genome into host cytosol. In human rhinovirus A2, this conversion is triggered by exposure to acid pH in the ...During infection, viruses undergo conformational changes that lead to delivery of their genome into host cytosol. In human rhinovirus A2, this conversion is triggered by exposure to acid pH in the endosome. The first subviral intermediate, the A-particle, is expanded and has lost the internal viral protein 4 (VP4), but retains its RNA genome. The nucleic acid is subsequently released, presumably through one of the large pores that open at the icosahedral twofold axes, and is transferred along a conduit in the endosomal membrane; the remaining empty capsids, termed B-particles, are shuttled to lysosomes for degradation. Previous structural analyses revealed important differences between the native protein shell and the empty capsid. Nonetheless, little is known of A-particle architecture or conformation of the RNA core. Using 3D cryo-electron microscopy and X-ray crystallography, we found notable changes in RNA-protein contacts during conversion of native virus into the A-particle uncoating intermediate. In the native virion, we confirmed interaction of nucleotide(s) with Trp(38) of VP2 and identified additional contacts with the VP1 N terminus. Study of A-particle structure showed that the VP2 contact is maintained, that VP1 interactions are lost after exit of the VP1 N-terminal extension, and that the RNA also interacts with residues of the VP3 N terminus at the fivefold axis. These associations lead to formation of a well-ordered RNA layer beneath the protein shell, suggesting that these interactions guide ordered RNA egress.
リンク	Proc Natl Acad Sci U S A / PubMed:24277846 / PubMed Central
手法	EM (単粒子) / X線回折
解像度	6.5 - 10.9 Å
構造データ	EMDB-2106: HRV2 empty native capsid 手法: EM (単粒子) / 解像度: 10.9 Å EMDB-2107: HRV2 full native capsid 手法: EM (単粒子) / 解像度: 8.2 Å EMDB-2108: HRV2 empty 135S particle 手法: EM (単粒子) / 解像度: 9.9 Å EMDB-2109: HRV2 full 135S particle 手法: EM (単粒子) / 解像度: 8.8 Å PDB-4l3b: X-ray structure of the HRV2 A particle uncoating intermediate 手法: X-RAY DIFFRACTION / 解像度: 6.5 Å
由来	human rhinovirus a2 (ライノウイルス)
キーワード	VIRUS / HRV2 capsid