1ZXM

Human Topo IIa ATPase/AMP-PNP

1ZXM の概要

• エントリーDOI: 10.2210/pdb1zxm/pdb
• 関連するPDBエントリー: 1ZXN
• 分子名称: DNA topoisomerase II, alpha isozyme, MAGNESIUM ION, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: ghkl nucleotide-binding fold, isomerase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P11388
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92382.07

構造登録者

Wei, H.,Ruthenburg, A.J.,Bechis, S.K.,Verdine, G.L. (登録日: 2005-06-08, 公開日: 2005-08-23, 最終更新日: 2024-02-14)

主引用文献

Wei, H.,Ruthenburg, A.J.,Bechis, S.K.,Verdine, G.L.
Nucleotide-dependent Domain Movement in the ATPase Domain of a Human Type IIA DNA Topoisomerase.
J.Biol.Chem., 280:37041-37047, 2005

PubMed Abstract: Type IIA DNA topoisomerases play multiple essential roles in the management of higher-order DNA structure, including modulation of topological state, chromosome segregation, and chromatin condensation. These diverse physiologic functions are all accomplished through a common molecular mechanism, wherein the protein catalyzes transient cleavage of a DNA duplex (the G-segment) to yield a double-stranded gap through which another duplex (the T-segment) is passed. The overall process is orchestrated by the opening and closing of molecular "gates" in the topoisomerase structure, which is regulated by ATP binding, hydrolysis, and release of ADP and inorganic phosphate. Here we present two crystal structures of the ATPase domain of human DNA topoisomerase IIalpha in different nucleotide-bound states. Comparison of these structures revealed rigid-body movement of the structural modules within the ATPase domain, suggestive of the motions of a molecular gate.

PubMed: 16100112
DOI: 10.1074/jbc.M506520200

実験手法

X-RAY DIFFRACTION (1.87 Å)