Probing the Role of the ATP-Operated Clamp in the Strand-Passage Reaction of DNA Gyrase

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 Å, suggesting it could accommodate a DNA helix. Computer-modelling studies of this cavity suggest that it contains a co...

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Veröffentlicht in:	Nucleic acids research 1996-12, Vol.24 (24), p.4868-4873
Hauptverfasser:	Tingey, Andrew P., Maxwell, Anthony
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Cloning, Molecular DNA Topoisomerases, Type I - metabolism DNA Topoisomerases, Type II - genetics DNA Topoisomerases, Type II - metabolism Molecular Probes Mutagenesis, Site-Directed
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