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

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

Virology - 5 Jun 2012

Meineke Birthe, Shuman Stewart

Abstract excerpt

Breakage of tRNA by Escherichia coli anticodon nuclease PrrC (EcoPrrC) underlies a host antiviral response to phage T4 infection. Expression of EcoPrrC is cytocidal in yeast, signifying that PrrC ribotoxicity crosses phylogenetic domain boundaries. EcoPrrC consists of an N-terminal NTPase module that resembles ABC transporters and a C-terminal nuclease module that is sui generis. PrrC homologs are prevalent in...

Read the complete abstract on PubMed

Topics

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

Share to Escherichia coli Proteins
Share to Gene Expression Regulation, Bacterial
Share to Plasmids

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

Share to Protein Conformation

Share to Protein Structure, Tertiary

Share to Ribonucleases

Share to Saccharomyces cerevisiae

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 22386822
DOI: 10.1016/j.virol.2012.02.008
PMCID: PMC3312988

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

Structure-function relations in the NTPase domain of the antiviral tRNA ribotoxin Escherichia coli PrrC.PMID 22386822Read ↗

PrrC-anticodon nuclease: functional organization of a prototypical bacterial restriction RNase.Semantic proximity Read ↗

Phage tRNAs evade tRNA-targeting host defenses through anticodon loop mutations.Semantic proximity Read ↗

A fungal anticodon nuclease ribotoxin exploits a secondary cleavage site to evade tRNA repair.Semantic proximity Read ↗

Identification of the catalytic motif of the microbial ribosome inactivating cytotoxin colicin E3.Semantic proximity Read ↗

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

Structure, Biology, and Therapeutic Application of Toxin–Antitoxin Systems in Pathogenic BacteriaSemantic proximity Read ↗

Starting a new chapter on class Ia ribonucleotide reductasesSemantic proximity Read ↗

Accurate target identification for Mycobacterium tuberculosis endoribonuclease toxins requires expression in their native hostSemantic proximity Read ↗

The wobble nucleotide-excising anticodon nuclease RloC is governed by the zinc-hook and DNA-dependent ATPase of its Rad50-like region.Semantic proximity Read ↗

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

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

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

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