3RLK

Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein, monoclinic crystal form

Summary for 3RLK

• Entry DOI: 10.2210/pdb3rlk/pdb
• Related: 3RLC
• Descriptor: A1 protein, TETRAETHYLENE GLYCOL (3 entities in total)
• Functional Keywords: beta-barrel, polyproline helix, structural protein
• Biological source: Enterobacteria phage Qbeta
• Total number of polymer chains: 1
• Total formula weight: 21988.82

Authors

Rumnieks, J.,Tars, K. (deposition date: 2011-04-19, release date: 2011-09-28, Last modification date: 2024-02-28)

Primary citation

Rumnieks, J.,Tars, K.
Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein
Protein Sci., 20:1707-1712, 2011

PubMed 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.

PubMed: 21805520
DOI: 10.1002/pro.704

Experimental method

X-RAY DIFFRACTION (1.76 Å)