title: Crystal structure of the read-through domain from bacteriophage Qβ A1 protein.
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.
authors.affiliation: Latvian Biomedical Research and Study Centre, Ratsupites 1, Riga LV-1067, Latvia. j.rumnieks@biomed.lu.lv
authors.forename: Janis
authors.initials: J
authors.lastname: Rumnieks
authors.forename: Kaspars
authors.initials: K
authors.lastname: Tars
mesh_terms: D017908:Allolevivirus / Q000737:chemistry*; D000595:Amino Acid Sequence; D036022:Capsid Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment
chemical_list: D036022:Capsid Proteins; C043366:coat protein, Bacteriophage Qbeta