7RPW

Archaeal DNA ligase and heterotrimeric PCNA in complex with adenylated DNA

7RPW の概要

• エントリーDOI: 10.2210/pdb7rpw/pdb
• 関連するPDBエントリー: 7RPO 7RPW 7RPX
• EMDBエントリー: 24618 24624 24625
• 分子名称: DNA polymerase sliding clamp 1, DNA polymerase sliding clamp 2, DNA polymerase sliding clamp 3, ... (9 entities in total)
• 機能のキーワード: dna ligase, pcna, cryo-em, ligase-dna complex, ligase/dna
• 由来する生物種: Saccharolobus solfataricus (Sulfolobus solfataricus); 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 184206.27

構造登録者

Sverzhinsky, A.,Pascal, J.M. (登録日: 2021-08-04, 公開日: 2021-11-17, 最終更新日: 2024-06-05)

主引用文献

Sverzhinsky, A.,Tomkinson, A.E.,Pascal, J.M.
Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase.
Structure, 30:371-, 2022

PubMed Abstract: DNA ligases act in the final step of many DNA repair pathways and are commonly regulated by the DNA sliding clamp proliferating cell nuclear antigen (PCNA), but there are limited insights into the physical basis for this regulation. Here, we use single-particle cryoelectron microscopy (cryo-EM) to analyze an archaeal DNA ligase and heterotrimeric PCNA in complex with a single-strand DNA break. The cryo-EM structures highlight a continuous DNA-binding surface formed between DNA ligase and PCNA that supports the distorted conformation of the DNA break undergoing repair and contributes to PCNA stimulation of DNA ligation. DNA ligase is conformationally flexible within the complex, with its domains fully ordered only when encircling the repaired DNA to form a stacked ring structure with PCNA. The structures highlight DNA ligase structural transitions while docked on PCNA, changes in DNA conformation during ligation, and the potential for DNA ligase domains to regulate PCNA accessibility to other repair factors.

PubMed: 34838188
DOI: 10.1016/j.str.2021.11.002

実験手法

ELECTRON MICROSCOPY (4.38 Å)