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4W92

Crystal structure of Bacillus subtilis cyclic-di-AMP riboswitch ydaO

4W92 の概要
エントリーDOI10.2210/pdb4w92/pdb
分子名称U1 small nuclear ribonucleoprotein A, C-di-AMP ribsoswitch, MAGNESIUM ION, ... (6 entities in total)
機能のキーワードriboswitch, cyclic-di-amp, protein-rna complex, rna binding protein-rna complex, rna binding protein/rna
由来する生物種Homo sapiens (Human)
詳細
細胞内の位置Nucleus: P09012
タンパク質・核酸の鎖数2
化学式量合計50532.19
構造登録者
Jones, C.P.,Ferre-D'Amare, A.R. (登録日: 2014-08-26, 公開日: 2014-10-22, 最終更新日: 2024-10-23)
主引用文献Jones, C.P.,Ferre-D'Amare, A.R.
Crystal structure of a c-di-AMP riboswitch reveals an internally pseudo-dimeric RNA.
Embo J., 33:2692-2703, 2014
Cited by
PubMed Abstract: Cyclic diadenosine monophosphate (c-di-AMP) is a second messenger that is essential for growth and homeostasis in bacteria. A recently discovered c-di-AMP-responsive riboswitch controls the expression of genes in a variety of bacteria, including important pathogens. To elucidate the molecular basis for specific binding of c-di-AMP by a gene-regulatory mRNA domain, we have determined the co-crystal structure of this riboswitch. Unexpectedly, the structure reveals an internally pseudo-symmetric RNA in which two similar three-helix-junction elements associate head-to-tail, creating a trough that cradles two c-di-AMP molecules making quasi-equivalent contacts with the riboswitch. The riboswitch selectively binds c-di-AMP and discriminates exquisitely against other cyclic dinucleotides, such as c-di-GMP and cyclic-AMP-GMP, via interactions with both the backbone and bases of its cognate second messenger. Small-angle X-ray scattering experiments indicate that global folding of the riboswitch is induced by the two bound cyclic dinucleotides, which bridge the two symmetric three-helix domains. This structural reorganization likely couples c-di-AMP binding to gene expression.
PubMed: 25271255
DOI: 10.15252/embj.201489209
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.209 Å)
構造検証レポート
Validation report summary of 4w92
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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