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

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

Biochemistry - 26 Aug 2008

Plantinga Matthew J, Korennykh Alexei V, Piccirilli Joseph A, Correll Carl C

Abstract excerpt

Restrictocin, a member of the alpha-sarcin family of site-specific endoribonucleases, uses electrostatic interactions to bind to the ribosome and to RNA oligonucleotides, including the minimal specific substrate, the sarcin/ricin loop (SRL) of 23S-28S rRNA. Restrictocin binds to the SRL by forming a ground-state E:S complex that is stabilized predominantly by Coulomb interactions and depends on neither the...

Read the complete abstract on PubMed

Topics

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

Share to Aspergillus
Share to Fungal Proteins
Share to Nucleic Acid Conformation

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

Share to Protein Structure, Secondary

Share to Ribonucleases

Share to Static Electricity

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 18672906
DOI: 10.1021/bi800592g
PMCID: PMC2646754

Genes

SRL

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

Electrostatic interactions guide the active site face of a structure-specific ribonuclease to its RNA substrate.PMID 18672906Read ↗

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

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

Dissection of the high rate constant for the binding of a ribotoxin to the ribosome.Semantic proximity Read ↗

Analysis by systematic deletion of amino acids of the action of the ribotoxin restrictocin.Semantic proximity Read ↗

Allosteric modulation of the Lon protease by effector binding and local chargesSemantic proximity Read ↗

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

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

RNA tertiary interactions mediate native collapse of a bacterial group I ribozyme.Semantic proximity Read ↗

Structural characterization of the RNase E S1 domain and identification of its oligonucleotide-binding and dimerization interfaces.Semantic proximity Read ↗

Active barnase variants with completely random hydrophobic cores.Semantic proximity Read ↗

The role of Glu73 of barnase in catalysis and the binding of barstar.Semantic proximity Read ↗

Two distinct regions on the surface of an RNA-binding domain are crucial for RNase E function.Semantic proximity Read ↗

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