Structure of AP205 coat protein reveals circular permutation in ssRNA bacteriophages

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Item Type:	Article
Title:	Structure of AP205 coat protein reveals circular permutation in ssRNA bacteriophages
Creators Name:	Shishovs, M., Rumnieks, J., Diebolder, C., Jaudzems, K., Andreas, L.B., Stanek, J., Kazaks, A., Kotelovica, S., Akopjana, I., Pintacuda, G., Koning, R.I. and Tars, K.
Abstract:	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.
Keywords:	RNA Bacteriophage, Leviviridae, Coat Protein, Virus-like Particle, Circular Permutation
Source:	Journal of Molecular Biology
ISSN:	0022-2836
Publisher:	Elsevier
Volume:	428
Number:	21
Page Range:	4267-4279
Date:	23 October 2016
Official Publication:	https://doi.org/10.1016/j.jmb.2016.08.025
PubMed:	View item in PubMed

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