- EMDB-24618: Archaeal DNA ligase and heterotrimeric PCNA in complex with non-l... -
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基本情報
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データベース: EMDB / ID: EMD-24618
タイトル
Archaeal DNA ligase and heterotrimeric PCNA in complex with non-ligatable DNA
マップデータ
Sharpened map
試料
複合体: Ternary complex of DNA Ligase with PCNA1-2-3 and non-ligatable DNA
タンパク質・ペプチド: DNA polymerase sliding clamp 1
タンパク質・ペプチド: DNA polymerase sliding clamp 2
タンパク質・ペプチド: DNA polymerase sliding clamp 3
DNA: Upstream strand DNA
DNA: Downstream strand DNA
DNA: Template strand DNA
タンパク質・ペプチド: DNA ligase
リガンド: MANGANESE (II) ION
リガンド: ADENOSINE MONOPHOSPHATE
機能・相同性
機能・相同性情報
DNA ligase (ATP) / DNA ligase (ATP) activity / DNA ligation / lagging strand elongation / DNA biosynthetic process / DNA polymerase processivity factor activity / leading strand elongation / regulation of DNA replication / mismatch repair / translesion synthesis ...DNA ligase (ATP) / DNA ligase (ATP) activity / DNA ligation / lagging strand elongation / DNA biosynthetic process / DNA polymerase processivity factor activity / leading strand elongation / regulation of DNA replication / mismatch repair / translesion synthesis / DNA recombination / cell division / DNA repair / DNA binding / ATP binding / metal ion binding 類似検索 - 分子機能
DNA ligase, ATP-dependent, bacterial/archaeal / : / DNA ligase, ATP-dependent / DNA ligase, ATP-dependent, N-terminal / DNA ligase, ATP-dependent, N-terminal domain superfamily / DNA ligase N terminus / ATP-dependent DNA ligase signature 2. / ATP-dependent DNA ligase AMP-binding site. / DNA ligase, ATP-dependent, C-terminal / ATP dependent DNA ligase C terminal region ...DNA ligase, ATP-dependent, bacterial/archaeal / : / DNA ligase, ATP-dependent / DNA ligase, ATP-dependent, N-terminal / DNA ligase, ATP-dependent, N-terminal domain superfamily / DNA ligase N terminus / ATP-dependent DNA ligase signature 2. / ATP-dependent DNA ligase AMP-binding site. / DNA ligase, ATP-dependent, C-terminal / ATP dependent DNA ligase C terminal region / DNA ligase, ATP-dependent, conserved site / ATP-dependent DNA ligase family profile. / DNA ligase, ATP-dependent, central / ATP dependent DNA ligase domain / Proliferating cell nuclear antigen, PCNA, conserved site / Proliferating cell nuclear antigen signature 1. / Proliferating cell nuclear antigen, PCNA / Proliferating cell nuclear antigen, PCNA, N-terminal / Proliferating cell nuclear antigen, PCNA, C-terminal / Proliferating cell nuclear antigen, N-terminal domain / Proliferating cell nuclear antigen, C-terminal domain / : / Nucleic acid-binding, OB-fold 類似検索 - ドメイン・相同性
DNA polymerase sliding clamp 3 / DNA polymerase sliding clamp 1 / DNA polymerase sliding clamp 2 / DNA ligase 類似検索 - 構成要素
生物種
Saccharolobus solfataricus (古細菌) / Homo sapiens (ヒト)
Natural Sciences and Engineering Research Council (NSERC, Canada)
RGPIN-2015-05776
米国
National Institutes of Health/National Cancer Institute (NIH/NCI)
CA92584
米国
引用
ジャーナル: Structure / 年: 2022 タイトル: Cryo-EM structures and biochemical insights into heterotrimeric PCNA regulation of DNA ligase. 著者: Aleksandr Sverzhinsky / Alan E Tomkinson / John M Pascal / 要旨: 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 ...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.