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7MLW

Burkholderia sp. TJI49 Guanidine-I riboswitch

7MLW の概要
エントリーDOI10.2210/pdb7mlw/pdb
分子名称Guanidine-I riboswitch, GUANIDINE, PHOSPHATE ION, ... (7 entities in total)
機能のキーワードriboswitch, guanidine, potassium, ion, a-minor, rna
由来する生物種Burkholderia sp. TJI49
タンパク質・核酸の鎖数1
化学式量合計42270.05
構造登録者
Trachman, R.J.,Ferre-D'Amare, A.R. (登録日: 2021-04-29, 公開日: 2022-01-12, 最終更新日: 2023-10-18)
主引用文献Trachman 3rd, R.J.,Ferre-D'Amare, A.R.
An uncommon [K + (Mg 2+ ) 2 ] metal ion triad imparts stability and selectivity to the Guanidine-I riboswitch.
Rna, 27:1257-1264, 2021
Cited by
PubMed Abstract: The widespread -I riboswitch class exemplifies divergent riboswitch evolution. To analyze how natural selection has diversified its versatile RNA fold, we determined the X-ray crystal structure of the -I subtype-1 (Guanidine-I) riboswitch aptamer domain. Differing from the previously reported structures of orthologs from and , our structure reveals a chelated K ion adjacent to two Mg ions in the guanidine-binding pocket. Thermal melting analysis shows that K chelation, which induces localized conformational changes in the binding pocket, improves guanidinium-RNA interactions. Analysis of ribosome structures suggests that the [K(Mg)] ion triad is uncommon. It is, however, reminiscent of metal ion clusters found in the active sites of ribozymes and DNA polymerases. Previous structural characterization of -I subtype-2 RNAs, which bind the effector ligands ppGpp and PRPP, indicate that in those paralogs, an adenine responsible for K chelation in the Guanidine-I riboswitch is replaced by a pyrimidine. This mutation results in a water molecule and Mg ion binding in place of the K ion. Thus, our structural analysis demonstrates how ion and solvent chelation tune divergent ligand specificity and affinity among -I riboswitches.
PubMed: 34257148
DOI: 10.1261/rna.078824.121
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 7mlw
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2025-07-23に公開中

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