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 doma...

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Bibliographic Details
Published in:Nature (London) 1991-06, Vol.351 (6328), p.624-629
Main Authors: Wigley, Dale B, Davies, Gideon J, Dodson, Eleanor J, Maxwell, Anthony, Dodson, Guy
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - metabolism
Adenylyl Imidodiphosphate - metabolism
Amino Acid Sequence
ATP
Binding Sites
Biochemistry
Biological and medical sciences
Crystalline structure
Crystallization
Deoxyribonucleic acid
DNA
DNA Topoisomerases, Type II - chemistry
DNA Topoisomerases, Type II - metabolism
E coli
Escherichia coli - enzymology
Fundamental and applied biological sciences. Psychology
Macromolecular Substances
Models, Molecular
Molecular biophysics
Protein Conformation
Proteins
Structure in molecular biology
X-Ray Diffraction - methods
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Summary: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/351624a0