Journal
SCIENCE
Volume 312, Issue 5777, Pages 1208-1211Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1128451
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Riboswitches are untranslated regions of messenger RNA, which adopt alternate structures, depending on the binding of specific metabolites. Such conformational switching regulates the expression of proteins involved in the biosynthesis of riboswitch substrates. Here, we present the 2.9 angstrom-resolution crystal structure of the eukaryotic Arobidopsis thaliana thiamine pyrophosphate (TPP)-specific riboswitch in complex with its natural ligand. The riboswitch specifically recognizes the TIPP via conserved residues located within two highly distorted parallel sensor helices. The structure provides the basis for understanding the reorganization of the riboswitch fold upon TPP binding and explains the mechanism of resistance to the antibiotic pyrithiamine.
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