Crystal structure of an N-terminal fragment of the DNA gyrase B protein

Nature. 1991 Jun 20;351(6328):624-9. doi: 10.1038/351624a0.


The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, complexed with a nonhydrolysable ATP analogue, has been solved at 2.5 A resolution. It consists of two domains, both containing novel protein folds. The protein fragment forms a dimer, whose N-terminal domains are responsible for ATP binding and hydrolysis. The C-terminal domains form the sides of a 20 A hole through the protein dimer which may play a role in DNA strand passage during the supercoiling reaction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Adenylyl Imidodiphosphate / metabolism
  • Amino Acid Sequence
  • Binding Sites
  • Crystallization
  • DNA Topoisomerases, Type II / chemistry*
  • DNA Topoisomerases, Type II / metabolism
  • Escherichia coli / enzymology*
  • Macromolecular Substances
  • Models, Molecular
  • Protein Conformation
  • X-Ray Diffraction / methods


  • Macromolecular Substances
  • Adenylyl Imidodiphosphate
  • Adenosine Triphosphate
  • DNA Topoisomerases, Type II