ArticleNucleic acids research2013
Structural insight into negative DNA supercoiling by DNA gyrase, a bacterial type 2A DNA topoisomerase.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 67 citations in OpenAlex.
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- From Infection to Tumor: Exploring the Therapeutic Potential of Ciprofloxacin Derivatives as Anticancer Agents.Pharmaceuticals (Basel, Switzerland) · 2025Review
- Microbial-based natural products as potential inhibitors targeting DNA gyrase B ofFrontiers in chemistry · 2025Article
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- Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.Nucleic acids research · 2024Article
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- Structural basis of DNA crossover capture byScience (New York, N.Y.) · 2024Article
- Using energy to go downhill-a genoprotective role for ATPase activity in DNA topoisomerase II.Nucleic acids research · 2024Article
- Integrative illustration of a JCVI-syn3A minimal cell.Journal of integrative bioinformatics · 2022Article
- What makes a type IIA topoisomerase a gyrase or a Topo IV?Nucleic acids research · 2021Review
- DNA topoisomerases: Advances in understanding of cellular roles and multi-protein complexes via structure-function analysis.BioEssays : news and reviews in molecular, cellular and developmental biology · 2021Review
- Towards Conformation-Sensitive Inhibition of Gyrase: Implications of Mechanistic Insight for the Identification and Improvement of Inhibitors.Molecules (Basel, Switzerland) · 2021Review
- A YoeB toxin cleaves both RNA and DNA.Scientific reports · 2021Article
- Quinolone Complexes with Lanthanide Ions: An Insight into their Analytical Applications and Biological Activity.Molecules (Basel, Switzerland) · 2020Review
- Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Nucleic acids research · 2020Article
- Functional interactions between gyrase subunits are optimized in a species-specific manner.The Journal of biological chemistry · 2020Article
- Structure-Function Analysis Reveals the Singularity of Plant Mitochondrial DNA Replication Components: A Mosaic and Redundant System.Plants (Basel, Switzerland) · 2019Review
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Authors and funding
7 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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