3ECC

Crystal structure of the DnaC helicase loader in complex with ADP-BeF3

3ECC の概要

• エントリーDOI: 10.2210/pdb3ecc/pdb
• 関連するPDBエントリー: 3EC2
• 分子名称: DNA replication protein DnaC, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: helicase loader, replication initiation factor, atp-binding, nucleotide-binding, replication
• 由来する生物種: Aquifex aeolicus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21765.82

構造登録者

Mott, M.L.,Erzberger, J.P.,Coons, M.M.,Berger, J. (登録日: 2008-08-29, 公開日: 2008-11-25, 最終更新日: 2024-02-21)

主引用文献

Mott, M.L.,Erzberger, J.P.,Coons, M.M.,Berger, J.M.
Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators.
Cell(Cambridge,Mass.), 135:623-634, 2008

PubMed Abstract: The loading of oligomeric helicases onto replication origins marks an essential step in replisome assembly. In cells, dedicated AAA+ ATPases regulate loading, however, the mechanism by which these factors recruit and deposit helicases has remained unclear. To better understand this process, we determined the structure of the ATPase region of the bacterial helicase loader DnaC from Aquifex aeolicus to 2.7 A resolution. The structure shows that DnaC is a close paralog of the bacterial replication initiator, DnaA, and unexpectedly shares an ability to form a helical assembly similar to that of ATP-bound DnaA. Complementation and ssDNA-binding assays validate the importance of homomeric DnaC interactions, while pull-down experiments show that the DnaC and DnaA AAA+ domains interact in a nucleotide-dependent manner. These findings implicate DnaC as a molecular adaptor that uses ATP-activated DnaA as a docking site for regulating the recruitment and correct spatial deposition of the DnaB helicase onto origins.

PubMed: 19013274
DOI: 10.1016/j.cell.2008.09.058

実験手法

X-RAY DIFFRACTION (2.7 Å)