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	Individual subunits of a rhinovirus causing common cold exhibit largely different protein-RNA contact site conformations.
ジャーナル・号・ページ	Commun Biol, Vol. 3, Issue 1, Page 537, Year 2020
掲載日	2020年9月29日
著者	Dieter Blaas /
PubMed 要旨	Rhinoviruses cause the common cold. They are icosahedral, built from sixty copies each of the capsid proteins VP1 through VP4 arranged in a pseudo T = 3 lattice. This shell encases a ss(+) RNA ...Rhinoviruses cause the common cold. They are icosahedral, built from sixty copies each of the capsid proteins VP1 through VP4 arranged in a pseudo T = 3 lattice. This shell encases a ss(+) RNA genome. Three-D classification of single and oligomeric asymmetric units computationally excised from a 2.9 Å cryo-EM density map of rhinovirus A89, showed that VP4 and the N-terminal extension of VP1 adopt different conformations within the otherwise identical 3D-structures. Analysis of up to sixty classes of single subunits and of six classes of subunit dimers, trimers, and pentamers revealed different orientations of the amino acid residues at the interface with the RNA suggesting that local asymmetry is dictated by disparities of the interacting nucleotide sequences. The different conformations escape detection by 3-D structure determination of entire virions with the conformational heterogeneity being only indicated by low density. My results do not exclude that the RNA follows a conserved assembly mechanism, contacting most or all asymmetric units in a specific way. However, as suggested by the gradual loss of asymmetry with increasing oligomerization and the 3D-structure of entire virions reconstructed by using Euler angles selected in the classification of single subunits, RNA path and/or folding likely differ from virion to virion.
リンク	Commun Biol / PubMed:32994533 / PubMed Central
手法	EM (単粒子)
解像度	2.9 Å
構造データ	EMDB-11618: Class 1 of three-dimensional classification of single asymmetric units of RV-A89 into six classes. The class averages reveal differences at the RNA/protein interfaces. 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-11619: Individual subunits of a rhinovirus causing common cold exhibit largely different protein-RNA contact site conformations 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-11620: Class 3 of three-dimensional classification of single asymmetric units of RV-A89 into six classes. The class averages reveal differences at the RNA/protein interfaces. 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-11621: Class 4 of three-dimensional classification of single asymmetric units of RV-A89 into six classes. The class averages reveal differences at the RNA/protein interfaces. 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-11622: Class 5 of three-dimensional classification of single asymmetric units of RV-A89 into six classes. The class averages reveal differences at the RNA/protein interfaces. 手法: EM (単粒子) / 解像度: 2.9 Å EMDB-11623: Class 6 of three-dimensional classification of single asymmetric units of RV-A89 into six classes. The class averages reveal differences at the RNA/protein interfaces. 手法: EM (単粒子) / 解像度: 2.9 Å