The 3.3 Å structure of a plant geminivirus using cryo-EM.
The 3.3 Å structure of a plant geminivirus using cryo-EM.
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DOI：
10.1038/s41467-018-04793-6
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发表时间：
2018-06-18
影响因子：
16.6
通讯作者：
Ranson NA
中科院分区：
文献类型：
--
作者：
Hesketh EL;Saunders K;Fisher C;Potze J;Stanley J;Lomonossoff GP;Ranson NA
双生病毒是威胁全球粮食安全的主要植物病原体。它们具有独特的结构，由两个不完整的二十面体颗粒构成，融合形成双衣壳。然而，尽管它们对农业经济和基本生物利益很重要，但如何在 3D 中实现这一点的细节仍然未知。在这里，我们使用单粒子冷冻电子显微镜以 3.3 Å 分辨率报告了 Ageratum 黄脉病毒的结构，以及原子模型，该模型显示单个衣壳蛋白 (CP) 的 N 末端采用了三种不同的构象，这对于构建双半体之间的界面至关重要。我们的图谱还包含与每个 CP 结合的约 7 个单链 DNA 碱基的密度，并且我们表明基因组和 CP 之间的相互作用在界面处与衣壳其余部分不同。有了额外的诱变数据，这表明 DNA 结合诱导的构象变化在指导成对衣壳的组装中发挥着核心作用。双生病毒是一种重要的植物病原体，导致全球粮食作物大量损失。在这里，作者描述了 Ageratum 黄脉病毒的高分辨率冷冻电镜结构，并揭示了单个衣壳蛋白序列如何采用构建双衣壳所需的不同构象的分子细节。
Geminiviruses are major plant pathogens that threaten food security globally. They have a unique architecture built from two incomplete icosahedral particles, fused to form a geminate capsid. However, despite their importance to agricultural economies and fundamental biological interest, the details of how this is realized in 3D remain unknown. Here we report the structure of Ageratum yellow vein virus at 3.3 Å resolution, using single-particle cryo-electron microscopy, together with an atomic model that shows that the N-terminus of the single capsid protein (CP) adopts three different conformations essential for building the interface between geminate halves. Our map also contains density for ~7 bases of single-stranded DNA bound to each CP, and we show that the interactions between the genome and CPs are different at the interface than in the rest of the capsid. With additional mutagenesis data, this suggests a central role for DNA binding-induced conformational change in directing the assembly of geminate capsids. Geminiviruses are an important plant pathogen that causes large food crop losses globally. Here the authors describe a high resolution cryo-EM structure of the Ageratum yellow vein virus and reveal the molecular details of how a single capsid protein sequence can adopt the different conformations needed to build that geminate capsid.
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影响因子：
5.6
作者：
Ford, Robert J.;Barker, Amy M.;Bakker, Saskia E.;Coutts, Robert H.;Ranson, Neil A.;Phillips, Simon E. V.;Pearson, Arwen R.;Stockley, Peter G.
通讯作者：
Stockley, Peter G.
影响因子：
5.4
作者：
Bakker SE;Groppelli E;Pearson AR;Stockley PG;Rowlands DJ;Ranson NA
通讯作者：
Ranson NA
影响因子：
5.6
作者：
LILJAS, L;UNGE, T;STRANDBERG, B
通讯作者：
STRANDBERG, B
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
影响因子：
3
作者：
Pettersen, EF;Goddard, TD;Ferrin, TE
通讯作者：
Ferrin, TE