Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages
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- 作者：Mihails Shishovs1 ; Janis Rumnieks1 ; Christoph Diebolder2 ; Kristaps Jaudzems3 ; Loren B. Andreas3 ; Jan Stanek3 ; Andris Kazaks1 ; Svetlana Kotelovica1 ; Inara Akopjana1 ; Guido Pintacuda3 ; Roman I. Koning2 ; 5 ; Kaspars Tars1 ; 4 ; kaspars@biomed.lu.lv" class="auth_mail" title="E-mail the corresponding author
- 关键词：ssRNA ; single-stranded RNA ; VLP ; virus-like particle ; MAS ; magic-angle spinning ; 3D ; three-dimensional ; SeMet ; selenomethionine Tobacco Etch Virus ; TEV ; cryo-EM ; cryo-electron microscopy
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：23 October 2016
- 年：2016
- 卷：428
- 期：21
- 页码：4267-4279
- 全文大小：1756 K
文摘
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Structure of phage AP205 virus-like particles solved by combined X-ray, solid state NMR, and cryo-EM studies
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AP205 displays a circular permutation compared to other phage coat proteins.
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Coat protein termini are very surface exposed and suitable for fusions.
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Intersubunit disulfide bonds are important for particle assembly and stability.