Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages

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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

class="label">•: Structure of phage AP205 virus-like particles solved by combined X-ray, solid state NMR, and cryo-EM studies
class="label">•: AP205 displays a circular permutation compared to other phage coat proteins.
class="label">•: Coat protein termini are very surface exposed and suitable for fusions.
class="label">•: Intersubunit disulfide bonds are important for particle assembly and stability.

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