1OYW

Structure of the RecQ Catalytic Core

1OYW の概要

• エントリーDOI: 10.2210/pdb1oyw/pdb
• 関連するPDBエントリー: 1OYY
• 分子名称: ATP-dependent DNA helicase, ZINC ION, MANGANESE (II) ION, ... (4 entities in total)
• 機能のキーワード: recq, helicase, winged helix, helix-turn-helix, atp binding, zn(2+) binding, hydrolase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 59600.87

構造登録者

Bernstein, D.A.,Zittel, M.C.,Keck, J.L. (登録日: 2003-04-07, 公開日: 2003-10-07, 最終更新日: 2024-11-20)

主引用文献

Bernstein, D.A.,Zittel, M.C.,Keck, J.L.
High-resolution structure of the E. coli RecQ helicase catalytic core
Embo J., 22:4910-4921, 2003

PubMed Abstract: RecQ family helicases catalyze critical genome maintenance reactions in bacterial and eukaryotic cells, playing key roles in several DNA metabolic processes. Mutations in recQ genes are linked to genome instability and human disease. To define the physical basis of RecQ enzyme function, we have determined a 1.8 A resolution crystal structure of the catalytic core of Escherichia coli RecQ in its unbound form and a 2.5 A resolution structure of the core bound to the ATP analog ATPgammaS. The RecQ core comprises four conserved subdomains; two of these combine to form its helicase region, while the others form unexpected Zn(2+)-binding and winged-helix motifs. The structures reveal the molecular basis of missense mutations that cause Bloom's syndrome, a human RecQ-associated disease. Finally, based on findings from the structures, we propose a mechanism for RecQ activity that could explain its functional coordination with topoisomerase III.

PubMed: 14517231
DOI: 10.1093/emboj/cdg500

実験手法

X-RAY DIFFRACTION (1.8 Å)