+Search query
-Structure paper
Title | Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages. |
---|---|
Journal, issue, pages | J Mol Biol, Vol. 428, Issue 21, Page 4267-4279, Year 2016 |
Publish date | Oct 23, 2016 |
Authors | Mihails Shishovs / Janis Rumnieks / Christoph Diebolder / Kristaps Jaudzems / Loren B Andreas / Jan Stanek / Andris Kazaks / Svetlana Kotelovica / Inara Akopjana / Guido Pintacuda / Roman I Koning / Kaspars Tars / |
PubMed 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- ...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. |
External links | J Mol Biol / PubMed:27591890 |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 1.73 - 6.0 Å |
Structure data | EMDB-4098, PDB-5lqp: PDB-5fs4: |
Chemicals | ChemComp-HOH: |
Source |
|
Keywords | VIRAL PROTEIN / SMALL RNA PHAGE / COAT PROTEIN / AP205 / VIRUS LIKE PARTICLE / RNA bacteriophage / Leviviridae / virus-like particle |