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

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Abstract
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 supercoiling reaction.