Summary for 4LVV
| Entry DOI | 10.2210/pdb4lvv/pdb |
| Related | 3SD3 4LVW 4LVX 4LVY 4LVZ 4LW0 |
| Descriptor | THF riboswitch, N-[4-({[(6S)-2-amino-5-formyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl}amino)benzoyl]-L-glutamic acid (3 entities in total) |
| Functional Keywords | aptamers, nucleotide, 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, s-adenosylmethionine, streptococcus mutans, terminator regions, genetic, tetrahydrofolates, thermodynamics, transcription, three-way junction, pseudoknot, regulation, ncrna, thf binding, mrna, rna |
| Total number of polymer chains | 1 |
| Total formula weight | 29796.02 |
| 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 (2.1 Å) |
Structure validation
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