- PDB-9f26: Crystal structure of the PriS_PriL-Rpa2WH ternary complex from P.... -
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基本情報
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データベース: PDB / ID: 9f26
タイトル
Crystal structure of the PriS_PriL-Rpa2WH ternary complex from P. abyssi
要素
DNA primase large subunit PriL
DNA primase small subunit PriS
RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination
キーワード
DNA BINDING PROTEIN / Replication protein A / ssDNA-Binding protein
機能・相同性
機能・相同性情報
primosome complex / DNA replication, synthesis of primer / DNA-directed RNA polymerase complex / DNA-directed RNA polymerase activity / 転移酵素; リンを含む基を移すもの; 核酸を移すもの / 4 iron, 4 sulfur cluster binding / DNA binding / metal ion binding 類似検索 - 分子機能
DNA primase large subunit PriL / DNA primase small subunit PriS / Replication factor A protein-like / DNA primase, small subunit, eukaryotic/archaeal / DNA primase, small subunit / DNA primase small subunit / DNA primase large subunit, eukaryotic/archaeal / Eukaryotic and archaeal DNA primase, large subunit / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain ...DNA primase large subunit PriL / DNA primase small subunit PriS / Replication factor A protein-like / DNA primase, small subunit, eukaryotic/archaeal / DNA primase, small subunit / DNA primase small subunit / DNA primase large subunit, eukaryotic/archaeal / Eukaryotic and archaeal DNA primase, large subunit / OB-fold nucleic acid binding domain, AA-tRNA synthetase-type / OB-fold nucleic acid binding domain / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性
RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination / DNA primase large subunit PriL / DNA primase small subunit PriS 類似検索 - 構成要素
ジャーナル: Nat Commun / 年: 2024 タイトル: Communication between DNA polymerases and Replication Protein A within the archaeal replisome. 著者: Markel Martínez-Carranza / Léa Vialle / Clément Madru / Florence Cordier / Ayten Dizkirici Tekpinar / Ahmed Haouz / Pierre Legrand / Rémy A Le Meur / Patrick England / Rémi Dulermo / J ...著者: Markel Martínez-Carranza / Léa Vialle / Clément Madru / Florence Cordier / Ayten Dizkirici Tekpinar / Ahmed Haouz / Pierre Legrand / Rémy A Le Meur / Patrick England / Rémi Dulermo / J Iñaki Guijarro / Ghislaine Henneke / Ludovic Sauguet / 要旨: 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. ...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.
A: DNA primase small subunit PriS B: DNA primase large subunit PriL C: RPA32 subunit of the hetero-oligomeric complex involved in homologous recombination ヘテロ分子