ArticleThe Journal of biological chemistry2010
Structural and thermodynamic characterization of Vibrio fischeri CcdB.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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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.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Beyond AMR and virulence databases: genome wide associations of closely relatedFrontiers in microbiology · 2026Article
- Friend or Foe: Protein Inhibitors of DNA Gyrase.Biology · 2024Review
- Whole Genome Sequencing and Pan-Genomic Analysis of Multidrug-ResistantMicroorganisms · 2023Article
- Crystallization and X-ray analysis of all of the players in the autoregulation of the ataRT toxin-antitoxin system.Acta crystallographica. Section F, Structural biology communications · 2018Article
- Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria.Toxins · 2016Review
- Substrate Recognition and Activity Regulation of the Escherichia coli mRNA Endonuclease MazF.The Journal of biological chemistry · 2016Article
- Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems.Frontiers in molecular biosciences · 2016Review
- Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics.Nucleic acids research · 2014Article
- Characterization of the phd-doc and ccd toxin-antitoxin cassettes from Vibrio superintegrons.Journal of bacteriology · 2013Article
- Vibrio cholerae ParE2 poisons DNA gyrase via a mechanism distinct from other gyrase inhibitors.The Journal of biological chemistry · 2010Article
- Solution structure and membrane binding of the toxin fst of the par addiction module.Biochemistry · 2010Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
CcdB(Vfi) from Vibrio fischeri is a member of the CcdB family of toxins that poison covalent gyrase-DNA complexes. In solution CcdB(Vfi) is a dimer that unfolds to the corresponding monomeric components in a two-state fashion. In the unfolded state, the monomer retains a partial secondary structure. This observation correlates well with the crystal and NMR structures of the protein, which show a dimer with a hydrophobic core crossing the dimer interface. In contrast to its F plasmid homologue, CcdB(Vfi) possesses a rigid dimer interface, and the apparent relative rotations of the two subunits are due to structural plasticity of the monomer. CcdB(Vfi) shows a number of non-conservative substitutions compared with the F plasmid protein in both the CcdA and the gyrase binding sites. Although variation in the CcdA interaction site likely determines toxin-antitoxin specificity, substitutions in the gyrase-interacting region may have more profound functional implications.
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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.