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

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.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Shishovs M,Rumnieks J,Diebolder C,Jaudzems K,Andreas LB,Stanek J,Kazaks A,Kotelovica S,Akopjana I,Pintacuda G,Koning RI,Tars K

doi

10.1016/j.jmb.2016.08.025

subject

Has Abstract

pub_date

2016-10-23 00:00:00

pages

4267-4279

issue

21

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(16)30345-X

journal_volume

428

pub_type

杂志文章

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