9F26
Crystal structure of the PriS_PriL-Rpa2WH ternary complex from P. abyssi
Summary for 9F26
| Entry DOI | 10.2210/pdb9f26/pdb |
| Descriptor | DNA primase small subunit PriS, DNA primase large subunit PriL, RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination, ... (4 entities in total) |
| Functional Keywords | replication protein a, ssdna-binding protein, dna binding protein |
| Biological source | Pyrococcus abyssi More |
| Total number of polymer chains | 3 |
| Total formula weight | 118151.30 |
| Authors | Madru, C.,Legrand, P.,Haouz, A.,Sauguet, L. (deposition date: 2024-04-22, release date: 2024-12-04, Last modification date: 2025-01-22) |
| Primary citation | Martinez-Carranza, M.,Vialle, L.,Madru, C.,Cordier, F.,Tekpinar, A.D.,Haouz, A.,Legrand, P.,Le Meur, R.A.,England, P.,Dulermo, R.,Guijarro, J.I.,Henneke, G.,Sauguet, L. Communication between DNA polymerases and Replication Protein A within the archaeal replisome. Nat Commun, 15:10926-10926, 2024 Cited by PubMed Abstract: Replication Protein A (RPA) plays a pivotal role in DNA replication by coating and protecting exposed single-stranded DNA, and acting as a molecular hub that recruits additional replication factors. We demonstrate that archaeal RPA hosts a winged-helix domain (WH) that interacts with two key actors of the replisome: the DNA primase (PriSL) and the replicative DNA polymerase (PolD). Using an integrative structural biology approach, combining nuclear magnetic resonance, X-ray crystallography and cryo-electron microscopy, we unveil how RPA interacts with PriSL and PolD through two distinct surfaces of the WH domain: an evolutionarily conserved interface and a novel binding site. Finally, RPA is shown to stimulate the activity of PriSL in a WH-dependent manner. This study provides a molecular understanding of the WH-mediated regulatory activity in central replication factors such as RPA, which regulate genome maintenance in Archaea and Eukaryotes. PubMed: 39738083DOI: 10.1038/s41467-024-55365-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.501 Å) |
Structure validation
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