Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages. - Université Claude Bernard Lyon 1 Accéder directement au contenu
Article Dans Une Revue Journal of Molecular Biology Année : 2016

Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

Résumé

AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in the other known single-stranded RNA phages. AP205 has a similar structure at the same location formed by N- and C-terminal beta-strands, making it a circular permutant compared to the other coat proteins. The permutation moves the coat protein termini to the most surface-exposed part of the assembled particle, which explains its increased tolerance to long N- and C-terminal fusions.
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Dates et versions

hal-01546489 , version 1 (24-06-2017)

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Mihails Shishovs, Jan Rumnieks, Christoph Diebolder, Kristaps Jaudzems, Loren B Andreas, et al.. Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.. Journal of Molecular Biology, 2016, 428 (21), pp.4267-4279. ⟨10.1016/j.jmb.2016.08.025⟩. ⟨hal-01546489⟩
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