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

Dimers of Thermus thermophilus elongation factor Ts are required for its function as a nucleotide exchange factor of elongation factor Tu.

European journal of biochemistry - 1 Jul 1998

Nesper M, Nock S, Sedlák E, Antalík M, Podhradský D, Sprinzl M

Abstract excerpt

Elongation factor Ts (EF-Ts) promotes the formation of active GTP-bound elongation factor Tu (EF-Tu) by accelerating the dissociation of GDP from the EF-Tu x GDP complex. Thermus thermophilus EF-Ts forms a dimer in solution, which is stabilised by interaction of a three-stranded antiparallel beta-sheet from each of the two EF-Ts molecules. A disulfide bridge and several hydrophobic interactions are the main...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Circular Dichroism

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

Share to Dimerization

Share to Hot Temperature

Share to Mutation

Share to Protein Binding

Share to Protein Structure, Secondary

Share to Thermodynamics

Source

Identifiers

PMID: 9692904
DOI: 10.1046/j.1432-1327.1998.2550081.x

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

Dimers of Thermus thermophilus elongation factor Ts are required for its function as a nucleotide exchange factor of elongation factor Tu.PMID 9692904Read ↗

Irreversible thermal denaturation of elongation factor Ts from Thermus thermophilus effect of the residual structure and intermonomer disulfide bond.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 ↗

Limited proteolysis and amino acid replacements in the effector region of Thermus thermophilus elongation factor Tu.Semantic proximity Read ↗

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

The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy.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 ↗

Expression of bovine mitochondrial elongation factor Ts in Escherichia coli and characterization of the heterologous complex formed with prokaryotic elongation factor Tu.Semantic proximity Read ↗

Mutations in the G-domain of elongation factor G from Thermus thermophilus affect both its interaction with GTP and fusidic acid.Semantic proximity Read ↗

Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms.Semantic proximity Read ↗

Identification of thermodynamically relevant interactions between EF-Tu and backbone elements of tRNA.Semantic proximity Read ↗

Significance of mutations on the structural perturbation of thymidylate synthase: implications for their involvement in subunit exchange.Semantic proximity Read ↗

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