ArticlePloS one2010
Structural insights into the quinolone resistance mechanism of Mycobacterium tuberculosis DNA gyrase.
Article in PloS one, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 148 citations in OpenAlex.
- Prevalence and Molecular Characterization of Second-Line Drugs Resistance among Multidrug-ResistantBioMed research international · 2017Trial
- Computational introspection of impact of mutation A90V and A90E in DNA gyrase a of Mycobacterium tuberculosis in developing resistance against Delafloxacin.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026Article
- AssessingbioRxiv : the preprint server for biology · 2026Article
- Identification of novel DNA gyrase B inhibitors inFrontiers in tuberculosis · 2026Article
- Key Proteins and Enzymatic Mechanisms Underlying Drug Resistance in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- An Rcs Stress-Based High-Throughput Screen Reveals Novel Gyrase Inhibitors as Indirect Inducers of Cell Envelope Stress in Gram-Negative Bacteria.ACS infectious diseases · 2025Article
- Different propensities for gate opening in gyrases and topoisomerase IV.Nucleic acids research · 2025Article
- Structure-based Virtual Screening and Hit Identification of Novel designed Quinazolin-4(3H)-one Derivatives as Antitubercular Agent against TargetsCurrent drug discovery technologies · 2025Article
- Signal Propagation in the ATPase Domain ofBiochemistry · 2024Article
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- Tackling Nontuberculous Mycobacteria by Repurposable Drugs and Potential Leads from Natural Products.Current topics in medicinal chemistry · 2024Review
- Transition metal homoeostasis is key to metabolism and drug tolerance ofnpj antimicrobials and resistance · 2024Article
- TargetingRSC medicinal chemistry · 2023Review
- Exploring Alternative Pathways to Target Bacterial Type II Topoisomerases Using NBTI Antibacterials: Beyond Halogen-Bonding Interactions.Antibiotics (Basel, Switzerland) · 2023Article
- The Structural Features of Novel Bacterial Topoisomerase Inhibitors That Define Their Activity on Topoisomerase IV.Journal of medicinal chemistry · 2022Review
- Molecular Characterization of Mycobacterium ulcerans DNA Gyrase and Identification of Mutations Reducing Susceptibility to QuinolonesAntimicrobial agents and chemotherapy · 2022Article
- Structurally Optimized Potent Dual-Targeting NBTI Antibacterials with an Enhanced Bifurcated Halogen-Bonding Propensity.ACS medicinal chemistry letters · 2021Article
- The within-host evolution of antimicrobial resistance in Mycobacterium tuberculosis.FEMS microbiology reviews · 2021Review
- Binding profile of protein-ligand inhibitor complex and structure based design of new potent compounds via computer-aided virtual screening.Journal of clinical tuberculosis and other mycobacterial diseases · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mycobacterium tuberculosis DNA gyrase, an indispensable nanomachine involved in the regulation of DNA topology, is the only type II topoisomerase present in this organism and is hence the sole target for quinolone action, a crucial drug active against multidrug-resistant tuberculosis. To understand at an atomic level the quinolone resistance mechanism, which emerges in extensively drug resistant tuberculosis, we performed combined functional, biophysical and structural studies of the two individual domains constituting the catalytic DNA gyrase reaction core, namely the Toprim and the breakage-reunion domains. This allowed us to produce a model of the catalytic reaction core in complex with DNA and a quinolone molecule, identifying original mechanistic properties of quinolone binding and clarifying the relationships between amino acid mutations and resistance phenotype of M. tuberculosis DNA gyrase. These results are compatible with our previous studies on quinolone resistance. Interestingly, the structure of the entire breakage-reunion domain revealed a new interaction, in which the Quinolone-Binding Pocket (QBP) is blocked by the N-terminal helix of a symmetry-related molecule. This interaction provides useful starting points for designing peptide based inhibitors that target DNA gyrase to prevent its binding to DNA.
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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.