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

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

Biophysical journal - 1 Dec 2010

Wieden Hans-Joachim, Mercier Evan, Gray John, Steed Brett, Yawney Davis

Abstract excerpt

Elongation factor (EF) Tu delivers aminoacyl-tRNAs to the actively translating bacterial ribosome in a GTP-hydrolysis-dependent process. Rapid recycling of EF-Tu, catalyzed by EF-Ts, is required for efficient protein synthesis in vivo. Here we report a combined theoretical and experimental approach aimed at identifying three-dimensional communication networks in EF-Tu. As an example, we focus on the mechanistic...

Read the complete abstract on PubMed

Topics

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

Share to Biocatalysis
Share to Enzyme Stability

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Hydrogen Bonding

Share to Mutant Proteins

Share to Peptide Elongation Factor Tu

Share to Peptide Elongation Factors

Source

Open in PubMed Open full text

Identifiers

PMID: 21112298
DOI: 10.1016/j.bpj.2010.10.013
PMCID: PMC2998634

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

A combined molecular dynamics and rapid kinetics approach to identify conserved three-dimensional communication networks in elongation factor Tu.PMID 21112298Read ↗

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

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

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 ↗

Structural insights into translational fidelity.Semantic proximity Read ↗

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

Labeled EF-Tus for rapid kinetic studies of pretranslocation complex formation.Semantic proximity Read ↗

Probing the reactivity of the GTP- and GDP-bound conformations of elongation factor Tu in complex with the antibiotic GE2270 A.Semantic proximity Read ↗

Bacterial elongation factors EF-Tu, their mutants, chimeric forms, and domains: isolation and purification.Semantic proximity Read ↗

Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots.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 ↗

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