9F28

Crystal structure of the heterodimeric primase from pyrococcus abyssi (deletion of the PriL-CTD domain)

Summary for 9F28

• Entry DOI: 10.2210/pdb9f28/pdb
• Descriptor: DNA primase small subunit PriS, DNA primase large subunit PriL, ZINC ION, ... (6 entities in total)
• Functional Keywords: dna primase, pris, pril, replication
• Biological source: Pyrococcus abyssi; More
• Total number of polymer chains: 2
• Total formula weight: 67403.19

Authors

Madru, C.,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

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: 39738083
DOI: 10.1038/s41467-024-55365-w

Experimental method

X-RAY DIFFRACTION (1.85 Å)