Conformational Changes in DNA Gyrase Revealed by Limited Proteolysis
Open Access
- 1 August 1998
- journal article
- Published by Elsevier BV
- Vol. 273 (35), 22606-22614
- https://doi.org/10.1074/jbc.273.35.22606
Abstract
No abstract availableKeywords
This publication has 35 references indexed in Scilit:
- DNA gyrase as a drug targetTrends in Microbiology, 1997
- Conversion of DNA gyrase into a conventional type II topoisomeraseProceedings of the National Academy of Sciences, 1996
- Nucleotide Binding to the 43-Kilodalton N-Terminal Fragment of the DNA Gyrase B ProteinBiochemistry, 1995
- Evidence for a conformational change in the DNA gyrase–DNA complex from hydroxyl radical footprintingNucleic Acids Research, 1994
- The 43-kilodalton N-terminal fragment of the DNA gyrase B protein hydrolyzes ATP and binds coumarin drugsBiochemistry, 1993
- Crystal structure of an N-terminal fragment of the DNA gyrase B proteinNature, 1991
- The C-terminal domain of theEscherichia coliDNA gyrase A subunit is a DNA-binding proteinNucleic Acids Research, 1991
- DNA Gyrase: Structure and FunctionCritical Reviews in Biochemistry and Molecular Biology, 1991
- DNA gyrase: purification and catalytic properties of a fragment of gyrase B protein.Proceedings of the National Academy of Sciences of the United States of America, 1979
- Micrococcus luteus DNA gyrase: active components and a model for its supercoiling of DNA.Proceedings of the National Academy of Sciences of the United States of America, 1978