Structure of AP205 coat protein reveals circular permutation in ssRNA bacteriophages

Item Type:	Article
Title:	Structure of AP205 coat protein reveals circular permutation in ssRNA bacteriophages
Creators Name:	Shishovs, M. and Rumnieks, J. and Diebolder, C. and Jaudzems, K. and Andreas, L.B. and Stanek, J. and Kazaks, A. and Kotelovica, S. and Akopjana, I. and Pintacuda, G. and 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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