- PDB-8aaj: Crystal structure of the Pyrococcus abyssi RPA (apo form) -
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基本情報
登録情報
データベース: PDB / ID: 8aaj
タイトル
Crystal structure of the Pyrococcus abyssi RPA (apo form)
要素
RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination
RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination
Replication factor A
キーワード
DNA BINDING PROTEIN / Replication protein A / ssDNA-Binding protein
機能・相同性
機能・相同性情報
response to ionizing radiation / double-strand break repair via homologous recombination / nucleic acid binding / chromosome, telomeric region / DNA binding / metal ion binding 類似検索 - 分子機能
Replication factor A / RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination / RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2023 タイトル: DNA-binding mechanism and evolution of replication protein A. 著者: Clément Madru / Markel Martínez-Carranza / Sébastien Laurent / Alessandra C Alberti / Maelenn Chevreuil / Bertrand Raynal / Ahmed Haouz / Rémy A Le Meur / Marc Delarue / Ghislaine Henneke ...著者: Clément Madru / Markel Martínez-Carranza / Sébastien Laurent / Alessandra C Alberti / Maelenn Chevreuil / Bertrand Raynal / Ahmed Haouz / Rémy A Le Meur / Marc Delarue / Ghislaine Henneke / Didier Flament / Mart Krupovic / Pierre Legrand / Ludovic Sauguet / 要旨: Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little is known about the structure of RPA in ...Replication Protein A (RPA) is a heterotrimeric single stranded DNA-binding protein with essential roles in DNA replication, recombination and repair. Little is known about the structure of RPA in Archaea, the third domain of life. By using an integrative structural, biochemical and biophysical approach, we extensively characterize RPA from Pyrococcus abyssi in the presence and absence of DNA. The obtained X-ray and cryo-EM structures reveal that the trimerization core and interactions promoting RPA clustering on ssDNA are shared between archaea and eukaryotes. However, we also identified a helical domain named AROD (Acidic Rpa1 OB-binding Domain), and showed that, in Archaea, RPA forms an unanticipated tetrameric supercomplex in the absence of DNA. The four RPA molecules clustered within the tetramer could efficiently coat and protect stretches of ssDNA created by the advancing replisome. Finally, our results provide insights into the evolution of this primordial replication factor in eukaryotes.
履歴
登録
2022年7月1日
登録サイト: PDBE / 処理サイト: PDBE
改定 1.0
2023年5月3日
Provider: repository / タイプ: Initial release
改定 1.1
2024年6月19日
Group: Data collection / カテゴリ: chem_comp_atom / chem_comp_bond
A: Replication factor A B: RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination C: RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination ヘテロ分子