Structure of a topoisomerase II-DNA-nucleotide complex reveals a new control mechanism for ATPase activity.

ABSTRACT: Type IIA topoisomerases control DNA supercoiling and disentangle chromosomes through a complex ATP-dependent strand-passage mechanism. Although a general framework exists for type IIA topoisomerase function, the architecture of the full-length enzyme has remained undefined. Here we present the structure of a fully catalytic Saccharomyces cerevisiae topoisomerase II homodimer complexed with DNA and a nonhydrolyzable ATP analog. 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 bound DNA and a conformational transducing element in the ATPase domain, which we show is critical for both DNA-stimulated ATP hydrolysis and global topoisomera

SUBMITTER: Schmidt BH 

PROVIDER: S-EPMC3492516 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature