Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Molecular basis of gyrase poisoning by the addiction toxin CcdB.

Journal of molecular biology - 20 May 2005

Dao-Thi Minh-Hoa, Van Melderen Laurence, De Genst Erwin, Afif Hassan, Buts Lieven, Wyns Lode, Loris Remy

Abstract excerpt

Gyrase is an ubiquitous bacterial enzyme that is responsible for disentangling DNA during DNA replication and transcription. It is the target of the toxin CcdB, a paradigm for plasmid addiction systems and related bacterial toxin-antitoxin systems. The crystal structure of CcdB and the dimerization domain of the A subunit of gyrase (GyrA14) dictates an open conformation for the catalytic domain of gyrase when...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacterial Toxins
Share to Catalytic Domain
Share to Crystallography

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dimerization

Share to DNA Gyrase

Share to F Factor

Share to Molecular Structure

Share to Topoisomerase II Inhibitors

Source

Identifiers

PMID: 15854646
DOI: 10.1016/j.jmb.2005.03.049

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular basis of gyrase poisoning by the addiction toxin CcdB.PMID 15854646Read ↗

Mechanism of CcdA-Mediated Rejuvenation of DNA Gyrase.Semantic proximity Read ↗

Crystal structure of CcdB, a topoisomerase poison from E. coli.Semantic proximity Read ↗

The interaction of DNA gyrase with the bacterial toxin CcdB: evidence for the existence of two gyrase-CcdB complexes.Semantic proximity Read ↗

Interactions of CcdB with DNA gyrase. Inactivation of Gyra, poisoning of the gyrase-DNA complex, and the antidote action of CcdA.Semantic proximity Read ↗

Structural and functional determinants inferred from deep mutational scans.Semantic proximity Read ↗

The ratio between CcdA and CcdB modulates the transcriptional repression of the ccd poison-antidote system.Semantic proximity Read ↗

Cell killing by the F plasmid CcdB protein involves poisoning of DNA-topoisomerase II complexes.Semantic proximity Read ↗

Ter-Seq: A high-throughput method to stabilize transient ternary complexes and measure associated kinetics.Semantic proximity Read ↗

Structural basis for sequence context-independent single-stranded DNA cytosine deamination by the bacterial toxin SsdASemantic proximity Read ↗

CcdA chaperones CcdB against irreversible misfolding and aggregation via a cotranslational folding mechanism.Semantic proximity Read ↗

F plasmid CcdB killer protein: ccdB gene mutants coding for non-cytotoxic proteins which retain their regulatory functions.Semantic proximity Read ↗

Assembly and function of a bacterial genotoxin.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.