Abstract
The crystal structure of a large fragment of yeast type II DNA topoisomerase reveals a heart-shaped dimeric protein with a large central hole. It provides a molecular model of the enzyme as an ATP-modulated clamp with two sets of jaws at opposite ends, connected by multiple joints. An enzyme with bound DNA can admit a second DNA duplex through one set of jaws, transport it through the cleaved first duplex, and expel it through the other set of jaws.
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Berger, J., Gamblin, S., Harrison, S. et al. Structure and mechanism of DNA topoisomerase II. Nature 379, 225–232 (1996). https://doi.org/10.1038/379225a0
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DOI: https://doi.org/10.1038/379225a0
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