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


Organic Chemistry: Current Research

Author(s): Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G

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Abstract 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. This article was published in Nature and referenced in Organic Chemistry: Current Research

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