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

Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3.

Protein science : a publication of the Protein Society - 1 Jun 2004

Walker Daniel, Lancaster Lorna, James Richard, Kleanthous Colin

Abstract excerpt

Colicin E3 is a cytotoxic ribonuclease that specifically cleaves 16S rRNA at the ribosomal A-site to abolish protein synthesis in sensitive Escherichia coli cells. We have performed extensive mutagenesis of the 96-residue colicin E3 cytotoxic domain (E3 rRNase), assayed mutant colicins for in vivo cytotoxicity, and tested the corresponding E3 rRNase domains for their ability to inactivate ribosome function in...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Catalytic Domain
Share to Colicins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cytotoxins

Share to Enzyme Stability

Share to Ribonucleases

Share to Ribosomes

Share to Spectrometry, Fluorescence

Source

Open in PubMed Open full text

Identifiers

PMID: 15133158
DOI: 10.1110/ps.04658504
PMCID: PMC2279995

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3.PMID 15133158Read ↗

On the interaction of colicin E3 with the ribosome.Semantic proximity Read ↗

Structure-function relations in the NTPase domain of the antiviral tRNA ribotoxin Escherichia coli PrrC.Semantic proximity Read ↗

Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein.Semantic proximity Read ↗

CdiA from Enterobacter cloacae delivers a toxic ribosomal RNase into target bacteria.Semantic proximity Read ↗

The ribotoxin restrictocin recognizes its RNA substrate by selective engagement of active site residues.Semantic proximity Read ↗

Identification of amino acids critical for the cytotoxicity of Shiga toxin 1 and 2 in Saccharomyces cerevisiae.Semantic proximity Read ↗

Identification of residues in the putative TolA box which are essential for the toxicity of the endonuclease toxin colicin E9.Semantic proximity Read ↗

Electrostatic interactions guide the active site face of a structure-specific ribonuclease to its RNA substrate.Semantic proximity Read ↗

Transcriptional profiling of colicin-induced cell death of Escherichia coli MG1655 identifies potential mechanisms by which bacteriocins promote bacterial diversity.Semantic proximity Read ↗

The electrostatic character of the ribosomal surface enables extraordinarily rapid target location by ribotoxins.Semantic proximity Read ↗

Involvement of loops L2 and L4 of ribonucleolytic toxin restrictocin in its functional activity.Semantic proximity Read ↗

Role of the basic character of alpha-sarcin's NH2-terminal beta-hairpin in ribosome recognition and phospholipid interaction.Semantic proximity Read ↗

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