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7K9C

Crystal structure of Bacillus halodurans OapB (iodine-derivative) at 1.0 A

7K9C の概要
エントリーDOI10.2210/pdb7k9c/pdb
関連するPDBエントリー7K9B
分子名称OLE-associated protein B, IODIDE ION (3 entities in total)
機能のキーワードribonucleoprotein complex, ole rna, rna binding protein, rna
由来する生物種Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
タンパク質・核酸の鎖数2
化学式量合計24786.75
構造登録者
Yang, Y.,Breaker, R.R. (登録日: 2020-09-29, 公開日: 2021-03-03, 最終更新日: 2024-03-06)
主引用文献Yang, Y.,Harris, K.A.,Widner, D.L.,Breaker, R.R.
Structure of a bacterial OapB protein with its OLE RNA target gives insights into the architecture of the OLE ribonucleoprotein complex.
Proc.Natl.Acad.Sci.USA, 118:-, 2021
Cited by
PubMed Abstract: The OLE (ornate, large, and extremophilic) RNA class is one of the most complex and well-conserved bacterial noncoding RNAs known to exist. This RNA is known to be important for bacterial responses to stress caused by short-chain alcohols, cold, and elevated Mg concentrations. These biological functions have been shown to require the formation of a ribonucleoprotein (RNP) complex including at least two protein partners: OLE-associated protein A (OapA) and OLE-associated protein B (OapB). OapB directly binds OLE RNA with high-affinity and specificity and is believed to assist in assembling the functional OLE RNP complex. To provide the atomic details of OapB-OLE RNA interaction and to potentially reveal previously uncharacterized protein-RNA interfaces, we determined the structure of OapB from alone and in complex with an OLE RNA fragment at resolutions of 1.0 Å and 2.0 Å, respectively. The structure of OapB exhibits a K-shaped overall architecture wherein its conserved KOW motif and additional unique structural elements of OapB form a bipartite RNA-binding surface that docks to the P13 hairpin and P12.2 helix of OLE RNA. These high-resolution structures elucidate the molecular contacts used by OapB to form a stable RNP complex and explain the high conservation of sequences and structural features at the OapB-OLE RNA-binding interface. These findings provide insight into the role of OapB in the assembly and biological function of OLE RNP complex and can guide the exploration of additional possible OLE RNA-binding interactions present in OapB.
PubMed: 33619097
DOI: 10.1073/pnas.2020393118
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1 Å)
構造検証レポート
Validation report summary of 7k9c
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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