4LW0

Structure of the THF riboswitch bound to adenine

4LW0 の概要

• エントリーDOI: 10.2210/pdb4lw0/pdb
• 関連するPDBエントリー: 3SD3 4LVV 4LVW 4LVX 4LVY 4LVZ
• 分子名称: THF riboswitch, ADENINE (3 entities in total)
• 機能のキーワード: 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, adenine binding, mrna
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28984.27

構造登録者

Trausch, J.J.,Batey, R.T. (登録日: 2013-07-26, 公開日: 2014-03-19, 最終更新日: 2024-02-28)

主引用文献

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

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: 24388757
DOI: 10.1016/j.chembiol.2013.11.012

実験手法

X-RAY DIFFRACTION (1.889 Å)