ArticleActa crystallographica. Section D, Biological crystallography2015
The role of monovalent cations in the ATPase reaction of DNA gyrase.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- Biological Evaluation and Computational Modelling Studies onCurrent pharmaceutical design · 2025Article
- 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
- Preparation and Characterization of Cumin Essential Oil Nanoemulsion (CEONE) as an Antibacterial Agent and Growth Promoter in Broilers: A Study on Efficacy, Safety, and Health Impact.Animals : an open access journal from MDPI · 2024Article
- Synthesis, Biological Properties, and Molecular Docking Study of Novel 1,2,3-Triazole-8-quinolinol Hybrids.ACS omega · 2024Article
- Direct synthesis, characterization,Royal Society open science · 2024Article
- Benzothiazole DNA gyrase inhibitors and their conjugates with siderophore mimics: design, synthesis and evaluation.RSC advances · 2024Article
- Exploring the 5-Substituted 2-Aminobenzothiazole-Based DNA Gyrase B Inhibitors Active against ESKAPE Pathogens.ACS omega · 2023Article
- Determination of Chemical Composition and Investigation of Biological Activities ofMolecules (Basel, Switzerland) · 2023Article
- A comprehensive structural analysis of the ATPase domain of human DNA topoisomerase II beta bound to AMPPNP, ADP, and the bisdioxopiperazine, ICRF193.Structure (London, England : 1993) · 2022Article
- Antibacterial, Antifungal, and Antioxidant Activities of Silver Nanoparticles Biosynthesized fromAntioxidants (Basel, Switzerland) · 2021Article
- Pentapeptide repeat protein QnrB1 requires ATP hydrolysis to rejuvenate poisoned gyrase complexes.Nucleic acids research · 2021Article
- Article
- 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
- Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity.The Journal of biological chemistry · 2018Article
- Efficient use of single molecule time traces to resolve kinetic rates, models and uncertainties.The Journal of chemical physics · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Four new crystal structures of the ATPase domain of the GyrB subunit of Escherichia coli DNA gyrase have been determined. One of these, solved in the presence of K(+), is the highest resolution structure reported so far for this domain and, in conjunction with the three other structures, reveals new insights into the function of this domain. Evidence is provided for the existence of two monovalent cation-binding sites: site 1, which preferentially binds a K(+) ion that interacts directly with the α-phosphate of ATP, and site 2, which preferentially binds an Na(+) ion and the functional significance of which is not clear. The crystallographic data are corroborated by ATPase data, and the structures are compared with those of homologues to investigate the broader conservation of these sites.
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