8AA9

Crystal structure of the Rpa1 AROD-OB-1 domains

Summary for 8AA9

• Entry DOI: 10.2210/pdb8aa9/pdb
• Descriptor: Replication factor A, DI(HYDROXYETHYL)ETHER, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: replication protein a, ssdna-binding protein, dna binding protein
• Biological source: Pyrococcus abyssi GE5
• Total number of polymer chains: 2
• Total formula weight: 45285.48

Authors

Madru, C.,Legrand, P.,Sauguet, L. (deposition date: 2022-06-30, release date: 2023-05-03, Last modification date: 2024-05-01)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)