1zxm Citations

Nucleotide-dependent domain movement in the ATPase domain of a human type IIA DNA topoisomerase.

J Biol Chem 280 37041-7 (2005)
Cited: 141 times
EuropePMC logo PMID: 16100112

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.

Reviews - 1zxm mentioned but not cited (5)

Articles - 1zxm mentioned but not cited (73)

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Reviews citing this publication (15)

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