5BTP

Fusobacterium ulcerans ZTP riboswitch bound to ZMP

5BTP の概要

• エントリーDOI: 10.2210/pdb5btp/pdb
• 分子名称: RNA (62-MER), MAGNESIUM ION, AMINOIMIDAZOLE 4-CARBOXAMIDE RIBONUCLEOTIDE, ... (5 entities in total)
• 機能のキーワード: rna
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49402.05

構造登録者

Jones, C.P.,Ferre-D'Amare, A.R. (登録日: 2015-06-03, 公開日: 2015-08-12, 最終更新日: 2024-03-06)

主引用文献

Jones, C.P.,Ferre-D'Amare, A.R.
Recognition of the bacterial alarmone ZMP through long-distance association of two RNA subdomains.
Nat.Struct.Mol.Biol., 22:679-685, 2015

PubMed Abstract: The bacterial alarmone 5-aminoimidazole-4-carboxamide riboside 5'-triphosphate (AICAR triphosphate or ZTP), derived from the monophosphorylated purine precursor ZMP, accumulates during folate starvation. ZTP regulates genes involved in purine and folate metabolism through a cognate riboswitch. The linker connecting this riboswitch's two subdomains varies in length by over 100 nucleotides. We report the cocrystal structure of the Fusobacterium ulcerans riboswitch bound to ZMP, which spans the two subdomains whose interface also comprises a pseudoknot and ribose zipper. The riboswitch recognizes the carboxamide oxygen of ZMP through an unprecedented inner-sphere coordination with a Mg(2+) ion. We show that the affinity of the riboswitch for ZMP is modulated by the linker length. Notably, ZMP can simultaneously bind to the two subdomains even when they are synthesized as separate RNAs. The ZTP riboswitch demonstrates how specific small-molecule binding can drive association of distant noncoding-RNA domains to regulate gene expression.

PubMed: 26280533
DOI: 10.1038/nsmb.3073

実験手法

X-RAY DIFFRACTION (2.816 Å)