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 of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.

Nature communications - 19 May 2017

Jomaa Ahmad, Fu Yu-Hsien Hwang, Boehringer Daniel, Leibundgut Marc, Shan Shu-Ou, Ban Nenad

Abstract excerpt

During co-translational protein targeting, the signal recognition particle (SRP) binds to the translating ribosome displaying the signal sequence to deliver it to the SRP receptor (SR) on the membrane, where the signal peptide is transferred to the translocon. Using electron cryo-microscopy, we have determined the structure of a quaternary complex of the translating Escherichia coli ribosome, the SRP-SR in the...

Read the complete abstract on PubMed

Topics

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

Share to Cryoelectron Microscopy
Share to Hydrophobic and Hydrophilic Interactions

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

Share to Molecular Docking Simulation

Share to Protein Sorting Signals

Share to Protein Structure, Quaternary

Share to Receptors, Cytoplasmic and Nuclear

Share to Receptors, Peptide

Share to Signal Recognition Particle

Source

Open in PubMed Open full text

Identifiers

PMID: 28524878
DOI: 10.1038/ncomms15470
PMCID: PMC5454536

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 of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.PMID 28524878Read ↗

Molecular mechanism of GTPase activation at the signal recognition particle (SRP) RNA distal end.Semantic proximity Read ↗

The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting.Semantic proximity Read ↗

Cryoelectron microscopy structures of the ribosome complex in intermediate states during tRNA translocation.Semantic proximity Read ↗

Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Semantic proximity Read ↗

Structured mRNAs regulate translation initiation by binding to the platform of the ribosome.Semantic proximity Read ↗

Ribosome. The complete structure of the 55S mammalian mitochondrial ribosome.Semantic proximity Read ↗

Dissecting the molecular organization of the translocon-associated protein complex.Semantic proximity Read ↗

Ensemble cryo-EM uncovers inchworm-like translocation of a viral IRES through the ribosomeSemantic proximity Read ↗

A molecular modeling study of the interaction between SRP-receptor complex and peptide translocon.Semantic proximity Read ↗

Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Semantic proximity Read ↗

Conformations of the signal recognition particle protein Ffh from Escherichia coli as determined by FRET.Semantic proximity Read ↗

SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.Semantic proximity Read ↗

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