Title: Crystal structure of an N-terminal fragment of the DNA gyrase B protein. | Journal: Nature. 1991 Jun;351(6328):624-9 | Authors: Wigley DB, Davies GJ, Dodson EJ, Maxwell A, Dodson G. | 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. | See full PubMed entry: http://www.ncbi.nlm.nih.gov/pubmed/1646964 |
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