4LVX
Structure of the THF riboswitch bound to tetrahydrobiopterin
Summary for 4LVX
| Entry DOI | 10.2210/pdb4lvx/pdb |
| Related | 3SD3 4LVV 4LVW 4LVY 4LVZ 4LW0 |
| Descriptor | THF riboswitch, 5,6,7,8-TETRAHYDROBIOPTERIN (3 entities in total) |
| Functional Keywords | aptamers, nucleotide, bacillus subtilis, bacterial proteins, base sequence, binding sites, calorimetry, folic acid, gene expression regulation, bacterial, guanine, leucovorin, ligands, magnesium, molecular sequence data, nucleic acid conformation, point mutation, protein binding, protein structure, secondary, rna, riboswitch, s-adenosylmethionine, streptococcus mutans, terminator regions, genetic, tetrahydrofolates, thermodynamics, transcription, three-way junction, pseudoknot, regulation, ncrna, tetrahydrobiopterin binding, mrna |
| Total number of polymer chains | 1 |
| Total formula weight | 29331.64 |
| Authors | Trausch, J.J.,Batey, R.T. (deposition date: 2013-07-26, release date: 2014-03-19, Last modification date: 2024-02-28) |
| Primary citation | Trausch, J.J.,Batey, R.T. A Disconnect between High-Affinity Binding and Efficient Regulation by Antifolates and Purines in the Tetrahydrofolate Riboswitch. Chem.Biol., 21:205-216, 2014 Cited by PubMed 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. PubMed: 24388757DOI: 10.1016/j.chembiol.2013.11.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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