ArticleRNA (New York, N.Y.)2013
Mechanism of activation of elongation factor Tu by ribosome: catalytic histidine activates GTP by protonation.
Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Human protein synthesis requires aminoacyl-tRNA pivoting during proofreading.Nature communications · 2025Article
- 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.Nucleic acids research · 2018Article
- Cyclization Reaction Catalyzed by Cyclodipeptide Synthases Relies on a Conserved Tyrosine Residue.Scientific reports · 2018Article
- EF-Tu and EF-G are activated by allosteric effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Mutations in the G-domain of Ski7 cause specific dysfunction in non-stop decay.Scientific reports · 2016Article
- Selenite Reduction by Anaerobic Microbial Aggregates: Microbial Community Structure, and Proteins Associated to the Produced Selenium Spheres.Frontiers in microbiology · 2016Article
- Tobramycin and bicarbonate synergise to kill planktonicNPJ biofilms and microbiomes · 2016Article
- Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome.Scientific reports · 2015Article
- Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.Nucleic acids research · 2015Article
- A monovalent cation acts as structural and catalytic cofactor in translational GTPases.The EMBO journal · 2014Article
- Ribosome-induced tuning of GTP hydrolysis by a translational GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Quantitative exploration of the molecular origin of the activation of GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 proposals, including those spurred by a recent X-ray crystallographic analysis of a ribosome:EF-Tu:aa-tRNA:GTP-analog complex. In this work, we have investigated these and alternative hypotheses, using high-level quantum chemical/molecular mechanical simulations for the wild-type protein and its His85Gln mutant. For both proteins, we find previously unsuggested mechanisms as being preferred, in which residue 85, either His or Gln, directly assists in the reaction. Analysis shows that the RNA has a minor catalytic effect in the wild-type reaction, but plays a significant role in the mutant by greatly stabilizing the reaction's transition state. Given the similarity between EF-Tu and other members of the translational G-protein family, it is likely that these mechanisms of ribosome-activated GTP hydrolysis are pertinent to all of these proteins.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.