期刊
NUCLEIC ACIDS RESEARCH
卷 41, 期 16, 页码 7815-7827出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt560
关键词
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资金
- European Community
- Alsace Region
- CNRS
- Fondation pour la Recherche Medicale
- national member subscriptions as well as the French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INSB-05-01]
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 beta-pinwheel domains and guided to introduce negative supercoils through cooperativity between the ATPase and beta-pinwheel domains. The overall conformation of the drug-induced DNA binding-cleavage complex also suggests that ciprofloxacin traps a DNA pre-transport conformation.
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