5LQP

Cryo-EM reconstruction of bacteriophage AP205 virus-like particles.

This is a non-PDB format compatible entry.

Summary for 5LQP

• Entry DOI: 10.2210/pdb5lqp/pdb
• EMDB information: 4098
• Descriptor: Coat protein (1 entity in total)
• Functional Keywords: rna bacteriophage, leviviridae, coat protein, virus-like particle, virus like particle
• Biological source: Acinetobacter phage AP205
• Total number of polymer chains: 180
• Total formula weight: 2487702.42

Authors

Diebolder, C.A.,Rumnieks, J.,Tars, K.,Koning, R.I. (deposition date: 2016-08-17, release date: 2016-12-14, Last modification date: 2024-10-16)

Primary citation

Shishovs, M.,Rumnieks, J.,Diebolder, C.,Jaudzems, K.,Andreas, L.B.,Stanek, J.,Kazaks, A.,Kotelovica, S.,Akopjana, I.,Pintacuda, G.,Koning, R.I.,Tars, K.
Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.
J. Mol. Biol., 428:4267-4279, 2016

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-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.

PubMed: 27591890
DOI: 10.1016/j.jmb.2016.08.025

Experimental method

ELECTRON MICROSCOPY (6 Å)