Structure and mechanism of DNA topoisomerase II

Nature. 1996 Jan 18;379(6562):225-32. doi: 10.1038/379225a0.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Triphosphatases / chemistry
  • Adenosine Triphosphatases / metabolism
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Crystallography, X-Ray
  • DNA / metabolism
  • DNA Gyrase
  • DNA Topoisomerases, Type II / chemistry*
  • DNA Topoisomerases, Type II / metabolism
  • Escherichia coli / enzymology
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism
  • Protein Binding
  • Protein Conformation
  • Saccharomyces cerevisiae / enzymology


  • Peptide Fragments
  • Adenosine Triphosphate
  • DNA
  • Adenosine Triphosphatases
  • DNA Gyrase
  • DNA Topoisomerases, Type II