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 inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein.

Journal of molecular biology - 28 Apr 2006

Luna-Chávez César, Lin Yi-Lun, Huang Raven H

Abstract excerpt

Colicin E5 is a tRNA-specific ribonuclease that recognizes and cleaves four tRNAs in Escherichia coli that contain the hypermodified nucleoside queuosine (Q) at the wobble position. Cells that produce colicin E5 also synthesize the cognate immunity protein (Im5) that rapidly and tightly associate...

Read the complete abstract on PubMed

Topics

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

Share to Colicins
Share to Crystallography, X-Ray
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Protein Conformation

Share to Ribonucleases

Share to RNA, Bacterial

Share to RNA, Transfer

Source

Identifiers

PMID: 16524591
DOI: 10.1016/j.jmb.2006.02.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16524591-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein.PMID 16524591Read ↗

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

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

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

Investigation of the specificity of the interaction between colicin E9 and its immunity protein by site-directed mutagenesis.Semantic proximity Read ↗

Interaction of C5 protein with RNA aptamers selected by SELEX.Semantic proximity Read ↗

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

Structural aspects of the inhibition of DNase and rRNase colicins by their immunity proteins.Semantic proximity Read ↗

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

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

M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.Semantic proximity Read ↗

Following evolutionary paths to protein-protein interactions with high affinity and selectivity.Semantic proximity Read ↗

Structural architecture of an RNA that competitively inhibits RNase L.Semantic proximity Read ↗

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