Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.
J Mol Biol
; 428(21): 4267-4279, 2016 10 23.
Article
en En
| MEDLINE
| ID: mdl-27591890
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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Virus ARN
/
Bacteriófagos
/
Proteínas de la Cápside
Idioma:
En
Revista:
J Mol Biol
Año:
2016
Tipo del documento:
Article
País de afiliación:
Letonia