ArticleNature structural & molecular biology2012
ATP binding controls distinct structural transitions of Escherichia coli DNA gyrase in complex with DNA.
Article in Nature structural & molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Biomanufacturing Potential of Streamlined Cells.Biotechnology and bioengineering · 2025Article
- Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Cochaperones convey the energy of ATP hydrolysis for directional action of Hsp90.Nature communications · 2024Article
- Embracing Heterogeneity: Challenging the Paradigm of Replisomes as Deterministic Machines.Chemical reviews · 2023Review
- spotter: a single-nucleotide resolution stochastic simulation model of supercoiling-mediated transcription and translation in prokaryotes.Nucleic acids research · 2023Article
- Twenty Years of Collaboration to Sort out Phage Mu Replication and Its Dependence on the Mu Central Gyrase Binding Site.Viruses · 2023Article
- Article
- Pentapeptide repeat protein QnrB1 requires ATP hydrolysis to rejuvenate poisoned gyrase complexes.Nucleic acids research · 2021Article
- Multiplex flow magnetic tweezers reveal rare enzymatic events with single molecule precision.Nature communications · 2020Article
- Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cas9 interrogates DNA in discrete steps modulated by mismatches and supercoiling.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Modulated control of DNA supercoiling balance by the DNA-wrapping domain of bacterial gyrase.Nucleic acids research · 2020Article
- DNA Topoisomerase Inhibitors: Trapping a DNA-Cleaving Machine in Motion.Journal of molecular biology · 2019Review
- Supercoil Levels inMicroorganisms · 2019Article
- CryoEM structures of open dimers of gyrase A in complex with DNA illuminate mechanism of strand passage.eLife · 2018Article
- Gyrase containing a single C-terminal domain catalyzes negative supercoiling of DNA by decreasing the linking number in steps of two.Nucleic acids research · 2018Article
- Dynamic coupling between conformations and nucleotide states in DNA gyrase.Nature chemical biology · 2018Article
- Topoisomerase VI senses and exploits both DNA crossings and bends to facilitate strand passage.eLife · 2018Article
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Authors and funding
4 authors.
Funding
Abstract
DNA gyrase is a molecular motor that harnesses the free energy of ATP hydrolysis to introduce negative supercoils into DNA. A critical step in this reaction is the formation of a chiral DNA wrap. Here we observe gyrase structural dynamics using a single-molecule assay in which gyrase drives the processive, stepwise rotation of a nanosphere attached to the side of a stretched DNA molecule. Analysis of rotational pauses and measurements of DNA contraction reveal multiple ATP-modulated structural transitions. DNA wrapping is coordinated with the ATPase cycle and proceeds by way of an unanticipated structural intermediate that dominates the kinetics of supercoiling. Our findings reveal a conformational landscape of loosely coupled transitions funneling the motor toward productive energy transduction, a feature that may be common to the reaction cycles of other DNA and protein remodeling machines.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.