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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / metabolism
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Adenylyl Imidodiphosphate / metabolism
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Amino Acid Sequence
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Binding Sites
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Crystallization
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DNA Topoisomerases, Type II / chemistry*
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DNA Topoisomerases, Type II / metabolism
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Escherichia coli / enzymology*
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Macromolecular Substances
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Models, Molecular
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Protein Conformation
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X-Ray Diffraction / methods
Substances
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Macromolecular Substances
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Adenylyl Imidodiphosphate
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Adenosine Triphosphate
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DNA Topoisomerases, Type II