1ZXN

Human DNA topoisomerase IIa ATPase/ADP

Summary for 1ZXN

• Entry DOI: 10.2210/pdb1zxn/pdb
• Related: 1ZXM
• Descriptor: DNA topoisomerase II, alpha isozyme, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: ghkl nucleotide-binding fold, isomerase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P11388
• Total number of polymer chains: 4
• Total formula weight: 184732.38

Authors

Wei, H.,Ruthenburg, A.J.,Bechis, S.K.,Verdine, G.L. (deposition date: 2005-06-08, release date: 2005-08-23, Last modification date: 2024-02-14)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.51 Å)