Nucleic Acids Research, Vol 24, Issue 24 4868-4873, Copyright © 1996 by Oxford University Press
AP Tingey and A Maxwell
The high-resolution structure of the 43 kDa N-terminal fragment of the DNA
gyrase B protein shows a large cavity within the protein dimer. The
approximate size of this cavity is 20 A, suggesting it could accommodate a
DNA helix. Computer-modelling studies of this cavity suggest that it
contains a constriction, reducing the width to approximately 13 A,
principally caused by the side chain of Arg286. We have used site-directed
mutagenesis to alter this residue to Gln. Gyrase bearing this mutation
shows virtually no supercoiling activity and near-normal relaxation and DNA
cleavage activities. The mutated protein has ATPase activity which cannot
be stimulated by DNA. These data support the proposed role of the 43 kDa
domain as an ATP-operated clamp which binds DNA during the supercoiling
cycle. The lack of DNA- dependent ATPase of the mutant may indicate that
binding of DNA within the clamp is a prerequisite for stimulation of the
ATPase activity.
ARTICLES
Probing the role of the ATP-operated clamp in the strand-passage reaction of DNA gyrase
Department of Biochemistry, University of Leicester, UK.
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