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

Mechanism of activation of elongation factor Tu by ribosome: catalytic histidine activates GTP by protonation.

RNA (New York, N.Y.) - 1 Sept 2013

Aleksandrov Alexey, Field Martin

Abstract excerpt

Elongation factor Tu (EF-Tu) is central to prokaryotic protein synthesis as it has the role of delivering amino-acylated tRNAs to the ribosome. Release of EF-Tu, after correct binding of the EF-Tu:aa-tRNA complex to the ribosome, is initiated by GTP hydrolysis. This reaction, whose mechanism is uncertain, is catalyzed by EF-Tu, but requires activation by the ribosome. There have been a number of mechanistic...

Read the complete abstract on PubMed

Topics

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

Share to Catalysis
Share to Guanosine Triphosphate
Share to Histidine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrolysis

Share to Peptide Elongation Factor Tu

Share to Quantum Theory

Share to Ribosomes

Share to RNA, Transfer

Source

Open in PubMed Open full text

Identifiers

PMID: 23864225
DOI: 10.1261/rna.040097.113
PMCID: PMC3753929

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanism of activation of elongation factor Tu by ribosome: catalytic histidine activates GTP by protonation.PMID 23864225Read ↗

Converting structural information into an allosteric-energy-based picture for elongation factor Tu activation by the ribosome.Semantic proximity Read ↗

Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.Semantic proximity Read ↗

EF-Tu and EF-G are activated by allosteric effects.Semantic proximity Read ↗

A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu.Semantic proximity Read ↗

The conformation of a catalytic loop is central to GTPase activity on the ribosome.Semantic proximity Read ↗

Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A.Semantic proximity Read ↗

GE2270A-resistant mutations in elongation factor Tu allow productive aminoacyl-tRNA binding to EF-Tu.GTP.GE2270A complexes.Semantic proximity Read ↗

Structural insights into translational fidelity.Semantic proximity Read ↗

Mutation of the conserved Gly94 and Gly126 in elongation factor Tu from Escherichia coli. Elucidation of their structural and functional roles.Semantic proximity Read ↗

Design and properties of efficient tRNA:EF-Tu FRET system for studies of ribosomal translation.Semantic proximity Read ↗

Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.Semantic proximity Read ↗

Functional analysis of the uL11 protein impact on translational machinery.Semantic proximity Read ↗

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