Summary information and primary citation
- PDB-id
- 4lvx; DSSR-derived features in text and JSON formats
- Class
- RNA
- Method
- X-ray (1.9 Å)
- Summary
- Structure of the thf riboswitch bound to tetrahydrobiopterin
- 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.
