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Literature summary for 5.6.2.2 extracted from

  • Schmidt, B.H.; Osheroff, N.; Berger, J.M.
    Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity (2012), Nat. Struct. Mol. Biol., 19, 1147-1154.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
AMP-PNP structure analysis of a fully-catalytic Saccharomyces cerevisiae topoisomerase II homodimer complexed with DNA and the nonhydrolyzable ATP analogue, overview. The enzyme adopts a domain-swapped configuration wherein the ATPase domain of one protomer sits atop the nucleolytic region of its partner subunit. This organization produces an unexpected interaction between the bound DNA and a conformational transducing element in the ATPase domain, which is critical for both DNA-stimulated ATP hydrolysis and global topoisomerase activity. Three dimerization interfaces can each exist in an associated or dissociated state, giving rise to significant conformational variability within a population Saccharomyces cerevisiae

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate is negatively-supercoiled plasmid DNA Saccharomyces cerevisiae ?
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 ?

Subunits

Subunits Comment Organism
homodimer
-
 Saccharomyces cerevisiae

Synonyms

Synonyms Comment Organism
Topoisomerase II
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 Saccharomyces cerevisiae
type IIA topoisomerase
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 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
ATP the K-loop couples DNA binding to ATPase activity Saccharomyces cerevisiae

General Information

General Information Comment Organism
additional information the K-loop couples DNA binding to ATPase activity Saccharomyces cerevisiae
physiological function type IIA topoisomerases control DNA supercoiling and disentangle chromosomes by a complex, ATP-dependent strand passage mechanism, control mechanism for ATPase activity, overview Saccharomyces cerevisiae