6DGD

PriA helicase bound to dsDNA of a DNA replication fork

6DGD の概要

• エントリーDOI: 10.2210/pdb6dgd/pdb
• 関連するPDBエントリー: 4NL4 6DCR
• 分子名称: Primosomal protein N', DNA (5'-D(P*AP*GP*CP*AP*CP*GP*CP*CP*GP*AP*CP*T)-3'), DNA (5'-D(P*GP*TP*CP*GP*GP*CP*GP*TP*GP*CP*TP*C)-3'), ... (7 entities in total)
• 機能のキーワード: dna replication restart, pria helicase, dna replication fork binding, dsdna, leading arm, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• 由来する生物種: Klebsiella pneumoniae; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 183644.43

構造登録者

Satyshur, K.A.,Windgassen, T.A.,Keck, J.L. (登録日: 2018-05-17, 公開日: 2018-09-05, 最終更新日: 2023-10-11)

主引用文献

Windgassen, T.A.,Leroux, M.,Satyshur, K.A.,Sandler, S.J.,Keck, J.L.
Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.
Proc. Natl. Acad. Sci. U.S.A., 115:E9075-E9084, 2018

PubMed Abstract: DNA replication restart, the essential process that reinitiates prematurely terminated genome replication reactions, relies on exquisitely specific recognition of abandoned DNA replication-fork structures. The PriA DNA helicase mediates this process in bacteria through mechanisms that remain poorly defined. We report the crystal structure of a PriA/replication-fork complex, which resolves leading-strand duplex DNA bound to the protein. Interaction with PriA unpairs one end of the DNA and sequesters the 3'-most nucleotide from the nascent leading strand into a conserved protein pocket. Cross-linking studies reveal a surface on the winged-helix domain of PriA that binds to parental duplex DNA. Deleting the winged-helix domain alters PriA's structure-specific DNA unwinding properties and impairs its activity in vivo. Our observations lead to a model in which coordinated parental-, leading-, and lagging-strand DNA binding provide PriA with the structural specificity needed to act on abandoned DNA replication forks.

PubMed: 30201718
DOI: 10.1073/pnas.1809842115

実験手法

X-RAY DIFFRACTION (2.823 Å)