9F2A

Pyrococcus abyssi PolD in complex with Rpa2 winged-helix domain class 2 (composite map)

9F2A の概要

• エントリーDOI: 10.2210/pdb9f2a/pdb
• EMDBエントリー: 50143
• 分子名称: DNA polymerase II small subunit, DNA polymerase II large subunit, RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination, ... (5 entities in total)
• 機能のキーワード: dna polymerase, archaea, replication, rpa
• 由来する生物種: Pyrococcus abyssi GE5; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 233945.64

構造登録者

Martinez-Carranza, M.,Sauguet, L. (登録日: 2024-04-22, 公開日: 2024-12-04, 最終更新日: 2025-07-02)

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

ELECTRON MICROSCOPY (2.91 Å)