Structural highlights
Publication Abstract from PubMed
Bacteriophage Qbeta 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 Qbeta A1 protein was determined at a resolution of 1.8 A. The domain consists of a heavily deformed five-stranded beta-barrel on one side of the protein and a beta-hairpin and a three-stranded beta-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.
Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein.,Rumnieks J, Tars K Protein Sci. 2011 Oct;20(10):1707-12. doi: 10.1002/pro.704. Epub 2011 Aug, 18. PMID:21805520[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Rumnieks J, Tars K. Crystal structure of the read-through domain from bacteriophage Qbeta A1 protein. Protein Sci. 2011 Oct;20(10):1707-12. doi: 10.1002/pro.704. Epub 2011 Aug, 18. PMID:21805520 doi:10.1002/pro.704
