8AAS

Crystal structure of the Pyrococcus abyssi RPA trimerization core bound to poly-dT20 ssDNA

8AAS の概要

• エントリーDOI: 10.2210/pdb8aas/pdb
• 分子名称: Replication factor A, RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination, RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination, ... (6 entities in total)
• 機能のキーワード: replication protein a, ssdna-binding protein, dna binding protein
• 由来する生物種: Pyrococcus abyssi GE5; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 75348.16

構造登録者

Madru, C.,Legrand, P.,Sauguet, L. (登録日: 2022-07-01, 公開日: 2023-05-03, 最終更新日: 2024-05-01)

主引用文献

Madru, C.,Martinez-Carranza, M.,Laurent, S.,Alberti, A.C.,Chevreuil, M.,Raynal, B.,Haouz, A.,Le Meur, R.A.,Delarue, M.,Henneke, G.,Flament, D.,Krupovic, M.,Legrand, P.,Sauguet, L.
DNA-binding mechanism and evolution of replication protein A.
Nat Commun, 14:2326-2326, 2023

PubMed Abstract: 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.

PubMed: 37087464
DOI: 10.1038/s41467-023-38048-w

実験手法

X-RAY DIFFRACTION (3.2 Å)