title: Crystal structure of an N-terminal fragment of the DNA gyrase B protein.
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.
authors.affiliation: Department of Chemistry, York University, Heslington, UK.
authors.forename: D B
authors.initials: DB
authors.lastname: Wigley
authors.forename: G J
authors.initials: GJ
authors.lastname: Davies
authors.forename: E J
authors.initials: EJ
authors.lastname: Dodson
authors.forename: A
authors.initials: A
authors.lastname: Maxwell
authors.forename: G
authors.initials: G
authors.lastname: Dodson
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism; D000266:Adenylyl Imidodiphosphate / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D003460:Crystallization; D004250:DNA Topoisomerases, Type II / Q000737:chemistry* / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008958:Models, Molecular; D011487:Protein Conformation; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D046911:Macromolecular Substances; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D004250:DNA Topoisomerases, Type II