ArticleNucleic acids research2018
E. coli elongation factor Tu bound to a GTP analogue displays an open conformation equivalent to the GDP-bound form.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 25 citations in OpenAlex.
- From planktonic to biofilm states: single-cell transcriptomics reveals metabolic reprogramming and cellular heterogeneity inBiofilm · 2026Article
- Diverse bacterial pattern recognition receptors sense the conserved phage proteome.bioRxiv : the preprint server for biology · 2026Article
- D81 Mutants Reveal Hidden EF-Tu Diversity while Natural Sequences Preserve Aspartate.Computational and structural biotechnology journal · 2026Article
- Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs.Nucleic acids research · 2025Article
- SURFS and AlphaFold Reveal Ribosome Footprint Shift Caused by EF-Tu D81 Mutation.bioRxiv : the preprint server for biology · 2025Article
- Unveiling the innovative green synthesis mechanism of selenium nanoparticles by exploiting intracellular protein elongation factor Tu fromJournal of Zhejiang University. Science. B · 2024Article
- Native ESI-MS and Collision-Induced Unfolding (CIU) of the Complex between Bacterial Elongation Factor-Tu and the Antibiotic Enacyloxin IIa.Journal of the American Society for Mass Spectrometry · 2024Article
- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop.Nucleic acids research · 2022Article
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Differential Contribution of Protein Factors and 70S Ribosome to Elongation.International journal of molecular sciences · 2021Article
- Elongation Factor Tu Switch I Element is a Gate for Aminoacyl-tRNA Selection.Journal of molecular biology · 2020Article
- tRNA Dissociation from EF-Tu after GTP Hydrolysis: Primary Steps and Antibiotic Inhibition.Biophysical journal · 2020Article
- Switch of the interactions between the ribosomal stalk and EF1A in the GTP- and GDP-bound conformations.Scientific reports · 2019Article
- Omnipresent Maxwell's demons orchestrate information management in living cells.Microbial biotechnology · 2019Article
- Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome.Nucleic acids research · 2018Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
According to the traditional view, GTPases act as molecular switches, which cycle between distinct 'on' and 'off' conformations bound to GTP and GDP, respectively. Translation elongation factor EF-Tu is a GTPase essential for prokaryotic protein synthesis. In its GTP-bound form, EF-Tu delivers aminoacylated tRNAs to the ribosome as a ternary complex. GTP hydrolysis is thought to cause the release of EF-Tu from aminoacyl-tRNA and the ribosome due to a dramatic conformational change following Pi release. Here, the crystal structure of Escherichia coli EF-Tu in complex with a non-hydrolysable GTP analogue (GDPNP) has been determined. Remarkably, the overall conformation of EF-Tu·GDPNP displays the classical, open GDP-bound conformation. This is in accordance with an emerging view that the identity of the bound guanine nucleotide is not 'locking' the GTPase in a fixed conformation. Using a single-molecule approach, the conformational dynamics of various ligand-bound forms of EF-Tu were probed in solution by fluorescence resonance energy transfer. The results suggest that EF-Tu, free in solution, may sample a wider set of conformations than the structurally well-defined GTP- and GDP-forms known from previous X-ray crystallographic studies. Only upon binding, as a ternary complex, to the mRNA-programmed ribosome, is the well-known, closed GTP-bound conformation, observed.
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