3Q51

Structural analysis of a class I PreQ1 riboswitch aptamer in the metabolite-free state.

3Q51 の概要

• エントリーDOI: 10.2210/pdb3q51/pdb
• 関連するPDBエントリー: 3GCA 3Q50
• 分子名称: PREQ1 RIBOSWITCH, SULFATE ION, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: preq1, preq0, rna, ribosomal binding site, aptamer, metabolite, pseudoknot, h-type, riboswitch
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10719.78

構造登録者

Wedekind, J.E.,Jenkins, J.L.,Krucinska, J. (登録日: 2010-12-26, 公開日: 2011-05-18, 最終更新日: 2023-09-13)

主引用文献

Jenkins, J.L.,Krucinska, J.,McCarty, R.M.,Bandarian, V.,Wedekind, J.E.
Comparison of a preQ1 riboswitch aptamer in metabolite-bound and free states with implications for gene regulation.
J.Biol.Chem., 286:24626-24637, 2011

PubMed Abstract: Riboswitches are RNA regulatory elements that govern gene expression by recognition of small molecule ligands via a high affinity aptamer domain. Molecular recognition can lead to active or attenuated gene expression states by controlling accessibility to mRNA signals necessary for transcription or translation. Key areas of inquiry focus on how an aptamer attains specificity for its effector, the extent to which the aptamer folds prior to encountering its ligand, and how ligand binding alters expression signal accessibility. Here we present crystal structures of the preQ(1) riboswitch from Thermoanaerobacter tengcongensis in the preQ(1)-bound and free states. Although the mode of preQ(1) recognition is similar to that observed for preQ(0), surface plasmon resonance revealed an apparent K(D) of 2.1 ± 0.3 nm for preQ(1) but a value of 35.1 ± 6.1 nm for preQ(0). This difference can be accounted for by interactions between the preQ(1) methylamine and base G5 of the aptamer. To explore conformational states in the absence of metabolite, the free-state aptamer structure was determined. A14 from the ceiling of the ligand pocket shifts into the preQ(1)-binding site, resulting in "closed" access to the metabolite while simultaneously increasing exposure of the ribosome-binding site. Solution scattering data suggest that the free-state aptamer is compact, but the "closed" free-state crystal structure is inadequate to describe the solution scattering data. These observations are distinct from transcriptional preQ(1) riboswitches of the same class that exhibit strictly ligand-dependent folding. Implications for gene regulation are discussed.

PubMed: 21592962
DOI: 10.1074/jbc.M111.230375

実験手法

X-RAY DIFFRACTION (2.85 Å)