4PHY

Functional conservation despite structural divergence in ligand-responsive RNA switches

Summary for 4PHY

• Entry DOI: 10.2210/pdb4phy/pdb
• Descriptor: RNA (26-MER), RNA (5'-R(*GP*CP*AP*GP*GP*AP*AP*CP*CP*GP*AP*GP*AP*GP*GP*CP*AP*CP*GP*C)-3'), MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: viral genome, internal ribosome entry site, translation, rna
• Biological source: Seneca valley virus; More
• Total number of polymer chains: 2
• Total formula weight: 14896.62

Authors

Boerneke, M.A.,Dibrov, S.M.,Hermann, T.H. (deposition date: 2014-05-07, release date: 2015-02-18, Last modification date: 2023-12-27)

Primary citation

Boerneke, M.A.,Dibrov, S.M.,Gu, J.,Wyles, D.L.,Hermann, T.
Functional conservation despite structural divergence in ligand-responsive RNA switches.
Proc.Natl.Acad.Sci.USA, 111:15952-15957, 2014

PubMed Abstract: An internal ribosome entry site (IRES) initiates protein synthesis in RNA viruses, including the hepatitis C virus (HCV). We have discovered ligand-responsive conformational switches in viral IRES elements. Modular RNA motifs of greatly distinct sequence and local secondary structure have been found to serve as functionally conserved switches involved in viral IRES-driven translation and may be captured by identical cognate ligands. The RNA motifs described here constitute a new paradigm for ligand-captured switches that differ from metabolite-sensing riboswitches with regard to their small size, as well as the intrinsic stability and structural definition of the constitutive conformational states. These viral RNA modules represent the simplest form of ligand-responsive mechanical switches in nucleic acids.

PubMed: 25349403
DOI: 10.1073/pnas.1414678111

Experimental method

X-RAY DIFFRACTION (3.1 Å)