Crystal structure of an N-terminal fragment of the DNA gyrase B protein.
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.
Wigley
D B
DB
Department of Chemistry, York University, Heslington, UK.
Davies
G J
GJ
Dodson
E J
EJ
Maxwell
A
A
Dodson
G
G
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
D046911:Macromolecular Substances; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D004250:DNA Topoisomerases, Type II