5FS4

Bacteriophage AP205 coat protein

Summary for 5FS4

• Entry DOI: 10.2210/pdb5fs4/pdb
• Descriptor: AP205 BACTERIOPHAGE COAT PROTEIN (2 entities in total)
• Functional Keywords: viral protein, small rna phage, coat protein, ap205
• Biological source: ACINETOBACTER PHAGE AP205
• Total number of polymer chains: 2
• Total formula weight: 28149.58

Authors

Shishovs, M.,Tars, K. (deposition date: 2015-12-29, release date: 2016-09-21, Last modification date: 2024-05-08)

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-, 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

X-RAY DIFFRACTION (1.73 Å)