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8OEJ

Extended RPA-DNA nucleoprotein filament

Summary for 8OEJ
Entry DOI10.2210/pdb8oej/pdb
EMDB information16826
DescriptorReplication factor A, RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination, RPA14 subunit of the hetero-oligomeric complex involved in homologous recombination, ... (5 entities in total)
Functional Keywordsdna replication, single strand dna-binding protein, rpa, dna binding protein
Biological sourcePyrococcus abyssi
More
Total number of polymer chains7
Total formula weight203519.49
Authors
Madru, C.,Martinez-Carranza, M.,Sauguet, L. (deposition date: 2023-03-10, release date: 2023-05-10, Last modification date: 2024-07-24)
Primary citationMadru, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (7.96 Å)
Structure validation

227111

數據於2024-11-06公開中

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