9F27
Solution structure of the Pyrococcus abyssi Rpa2 winged-helix domain
Summary for 9F27
| Entry DOI | 10.2210/pdb9f27/pdb |
| NMR Information | BMRB: 34913 |
| Descriptor | RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination (1 entity in total) |
| Functional Keywords | winged-helix domain, polymerase pold interaction, primase prisl interaction, disordered linker, replication |
| Biological source | Pyrococcus abyssi GE5 |
| Total number of polymer chains | 1 |
| Total formula weight | 11006.38 |
| Authors | Le Meur, R.A.,Madru, C.,Cordier, F.,Sauguet, L.,Guijarro, J.I. (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 | SOLUTION NMR |
Structure validation
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