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

Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I.

Nucleic acids research - 1 Feb 2008

Cheng Bokun, Sorokin Elena P, Tse-Dinh Yuk-Ching

Abstract excerpt

The TOPRIM DXDXXG residues of type IA and II topoisomerases are involved in Mg(II) binding and the cleavage-rejoining of DNA. Mutation of the strictly conserved glycine to serine in Yersinia pestis and Escherichia coli topoisomerase I results in bacterial cell killing due to inhibition of DNA religation after DNA cleavage. In this study, all other substitutions at the TOPRIM glycine of Y. pestis topoisomerase I...

Read the complete abstract on PubMed

Topics

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

Share to DNA Topoisomerases, Type I
Share to Glycine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Magnesium

Share to Methionine

Share to SOS Response, Genetics

Share to Tyrosine

Share to Valine

Share to Yersinia pestis

Source

Open in PubMed Open full text

Identifiers

PMID: 18096618
DOI: 10.1093/nar/gkm1126
PMCID: PMC2241903

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutation adjacent to the active site tyrosine can enhance DNA cleavage and cell killing by the TOPRIM Gly to Ser mutant of bacterial topoisomerase I.PMID 18096618Read ↗

Bacterial topoisomerase I as a target for discovery of antibacterial compounds.Semantic proximity Read ↗

Bacterial cell killing mediated by topoisomerase I DNA cleavage activity.Semantic proximity Read ↗

Deciphering the distinct role for the metal coordination motif in the catalytic activity of Mycobacterium smegmatis topoisomerase I.Semantic proximity Read ↗

Inhibition of type IA topoisomerase by a monoclonal antibody through perturbation of DNA cleavage-religation equilibrium.Semantic proximity Read ↗

DNA replication proteins as potential targets for antimicrobials in drug-resistant bacterial pathogensSemantic proximity Read ↗

Type II topoisomerases--inhibitors, repair mechanisms and mutations.Semantic proximity Read ↗

Biochemical characterization of the topoisomerase domain of Methanopyrus kandleri topoisomerase V.Semantic proximity Read ↗

DNA Topoisomerases and Their Poisoning by Anticancer and Antibacterial DrugsSemantic proximity Read ↗

Mutational analysis of a type II topoisomerase cleavage site: distinct requirements for enzyme and inhibitors.Semantic proximity Read ↗

Drug Interactions with <i>Bacillus anthracis</i> Topoisomerase IV: Biochemical Basis for Quinolone Action and ResistanceSemantic proximity Read ↗

A new class of antibacterials, the imidazopyrazinones, reveal structural transitions involved in DNA gyrase poisoning and mechanisms of resistance.Semantic proximity Read ↗

DNA nicking by Escherichia coli topoisomerase IV with a substitution mutation from tyrosine to histidine at the active site.Semantic proximity Read ↗

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