ArticleNucleic acids research2013
Structure of an 'open' clamp type II topoisomerase-DNA complex provides a mechanism for DNA capture and transport.
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, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
41 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.
- Plasmid-mediated quinolone resistance in Enterobacteriaceae: a systematic review with a focus on Mediterranean countries.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2017Pooled it
- Phage-quinolone synergy: mechanisms, clinical strategies, and translational prospects.Frontiers in microbiology · 2026Review
- Molecular detection of blaSHV gene in multidrug resistance ofOpen veterinary journal · 2025Article
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- Mutagenesis of Intrinsically Disordered Domain Impacts Topoisomerase IIα Catalytic Activity.International journal of molecular sciences · 2025Article
- Advances in research on malignant tumors and targeted agents for TOP2A (Review).Molecular medicine reports · 2025Review
- Topoisomerase II N-terminal ATPase Clamp Stabilization.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural basis for difunctional mechanism of m-AMSA against African swine fever virus pP1192R.Nucleic acids research · 2024Article
- Experimental localization of metal-binding sites reveals the role of metal ions in type II DNA topoisomerases.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural insights into the assembly of type IIA topoisomerase DNA cleavage-religation center.Nucleic acids research · 2024Article
- Structure-function analysis of the ATPase domain of African swine fever virus topoisomerase.mBio · 2024Article
- Evolution of Resistance against Ciprofloxacin, Tobramycin, and Trimethoprim/Sulfamethoxazole in the Environmental Opportunistic PathogenAntibiotics (Basel, Switzerland) · 2024Article
- A unified view on enzyme catalysis by cryo-EM study of a DNA topoisomerase.Communications chemistry · 2024Article
- Article
- Review
- Unveiling the interdomain dynamics of type II DNA topoisomerase through all-atom simulations: Implications for understanding its catalytic cycle.Computational and structural biotechnology journal · 2023Article
- Integrative illustration of a JCVI-syn3A minimal cell.Journal of integrative bioinformatics · 2022Article
- The resistance mechanisms of bacteria against ciprofloxacin and new approaches for enhancing the efficacy of this antibiotic.Frontiers in public health · 2022Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Type II topoisomerases regulate DNA supercoiling and chromosome segregation. They act as ATP-operated clamps that capture a DNA duplex and pass it through a transient DNA break in a second DNA segment via the sequential opening and closure of ATPase-, G-DNA- and C-gates. Here, we present the first 'open clamp' structures of a 3-gate topoisomerase II-DNA complex, the seminal complex engaged in DNA recognition and capture. A high-resolution structure was solved for a (full-length ParE-ParC55)2 dimer of Streptococcus pneumoniae topoisomerase IV bound to two DNA molecules: a closed DNA gate in a B-A-B form double-helical conformation and a second B-form duplex associated with closed C-gate helices at a novel site neighbouring the catalytically important β-pinwheel DNA-binding domain. The protein N gate is present in an 'arms-wide-open' state with the undimerized N-terminal ParE ATPase domains connected to TOPRIM domains via a flexible joint and folded back allowing ready access both for gate and transported DNA segments and cleavage-stabilizing antibacterial drugs. The structure shows the molecular conformations of all three gates at 3.7 Å, the highest resolution achieved for the full complex to date, and illuminates the mechanism of DNA capture and transport by a type II topoisomerase.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.