Crystal structure of the read-through domain from bacteriophage Qβ A1 protein

Protein Sci. 2011 Oct;20(10):1707-12. doi: 10.1002/pro.704. Epub 2011 Aug 18.

Abstract

Bacteriophage Qβ is a small RNA virus that infects Escherichia coli. The virus particle contains a few copies of the minor coat protein A1, a C-terminally prolonged version of the coat protein, which is formed when ribosomes occasionally read-through the leaky stop codon of the coat protein. The crystal structure of the read-through domain from bacteriophage Qβ A1 protein was determined at a resolution of 1.8 Å. The domain consists of a heavily deformed five-stranded β-barrel on one side of the protein and a β-hairpin and a three-stranded β-sheet on the other. Several short helices and well-ordered loops are also present throughout the protein. The N-terminal part of the read-through domain contains a prominent polyproline type II helix. The overall fold of the domain is not similar to any published structure in the Protein Data Bank.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allolevivirus / chemistry*
  • Amino Acid Sequence
  • Capsid Proteins / chemistry*
  • Crystallography, X-Ray
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Sequence Alignment

Substances

  • Capsid Proteins
  • coat protein, Bacteriophage Qbeta

Associated data

  • PDB/3RLC
  • PDB/3RLK