Summary information and primary citation

PDB-id
4lw0; DSSR-derived features in text and JSON formats
Class
RNA
Method
X-ray (1.889 Å)
Summary
Structure of the thf riboswitch bound to adenine
Reference
Trausch JJ, Batey RT (2014): "A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch." Chem.Biol., 21, 205-216. doi: 10.1016/j.chembiol.2013.11.012.
Abstract
The tetrahydrofolate (THF) riboswitch regulates folate transport and metabolism in a number of Firmicutes by cooperatively binding two molecules of THF. To further understand this riboswitch's specificity for THF, binding and regulatory activity of a series of THF analogs and antifolates were examined. Our data reveal that although binding is dominated by the RNA's interactions with the pterin moiety, the para-aminobenzoic acid (pABA) moiety plays a significant role in transcriptional regulation. Further, we find that adenine and several other analogs bind with high affinity by an alternative binding mechanism. Despite a similar affinity to THF, adenine is a poor regulator of transcriptional attenuation. These results demonstrate that binding alone does not determine a compound's effectiveness in regulating the activity of the riboswitch-a complication in current efforts to develop antimicrobials that target these RNAs.

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