9F27

Solution structure of the Pyrococcus abyssi Rpa2 winged-helix domain

9F27 の概要

• エントリーDOI: 10.2210/pdb9f27/pdb
• NMR情報: BMRB: 34913
• 分子名称: RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination (1 entity in total)
• 機能のキーワード: winged-helix domain, polymerase pold interaction, primase prisl interaction, disordered linker, replication
• 由来する生物種: Pyrococcus abyssi GE5
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11006.38

構造登録者

Le Meur, R.A.,Madru, C.,Cordier, F.,Sauguet, L.,Guijarro, J.I. (登録日: 2024-04-22, 公開日: 2024-12-04, 最終更新日: 2025-01-22)

主引用文献

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

実験手法

SOLUTION NMR