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

@article{Wigley1991CrystalSO,
  title={Crystal structure of an N-terminal fragment of the DNA gyrase B protein},
  author={D. Wigley and G. Davies and E. Dodson and A. Maxwell and G. Dodson},
  journal={Nature},
  year={1991},
  volume={351},
  pages={624-629}
}
The crystal structure of an N-terminal fragment of the Escherichia coli DNA gyrase B protein, com-plexed with a nonhn/drolysable ATP analogue, has been solved at 2.5 Å 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 Å hole through the protein dimer which may play a role in DNA strand passage during the… Expand

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