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TitleStructural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase.
Journal, issue, pagesNucleic Acids Res, Vol. 41, Issue 16, Page 7815-7827, Year 2013
Publish dateJun 26, 2013
AuthorsJulie Papillon / Jean-François Ménétret / Claire Batisse / Reynald Hélye / Patrick Schultz / Noëlle Potier / Valérie Lamour /
PubMed AbstractType 2A DNA topoisomerases (Topo2A) remodel DNA topology during replication, transcription and chromosome segregation. These multisubunit enzymes catalyze the transport of a double-stranded DNA ...Type 2A DNA topoisomerases (Topo2A) remodel DNA topology during replication, transcription and chromosome segregation. These multisubunit enzymes catalyze the transport of a double-stranded DNA through a transient break formed in another duplex. The bacterial DNA gyrase, a target for broad-spectrum antibiotics, is the sole Topo2A enzyme able to introduce negative supercoils. We reveal here for the first time the architecture of the full-length Thermus thermophilus DNA gyrase alone and in a cleavage complex with a 155 bp DNA duplex in the presence of the antibiotic ciprofloxacin, using cryo-electron microscopy. The structural organization of the subunits of the full-length DNA gyrase points to a central role of the ATPase domain acting like a 'crossover trap' that may help to sequester the DNA positive crossover before strand passage. Our structural data unveil how DNA is asymmetrically wrapped around the gyrase-specific C-terminal β-pinwheel domains and guided to introduce negative supercoils through cooperativity between the ATPase and β-pinwheel domains. The overall conformation of the drug-induced DNA binding-cleavage complex also suggests that ciprofloxacin traps a DNA pre-transport conformation.
External linksNucleic Acids Res / PubMed:23804759 / PubMed Central
MethodsEM (single particle)
Resolution16.8 - 23.0 Å
Structure data

EMDB-2360:
Electron cryo-EM of full-length Thermus thermophilus DNA gyrase
Method: EM (single particle) / Resolution: 16.8 Å

EMDB-2361:
Electron cryo-EM of the full-length Thermus thermophilus DNA gyrase in complex with a 155bp DNA and ciprofloxacin
Method: EM (single particle) / Resolution: 23.0 Å

Source
  • Thermus thermophilus (bacteria)
  • Escherichia coli (E. coli)

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