ArticleNature communications2013
Energetics of activation of GTP hydrolysis on the ribosome.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 59 citations in OpenAlex.
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- Translational reprogramming as a driver of antimony-drug resistance in Leishmania.Nature communications · 2023Article
- A topological data analytic approach for discovering biophysical signatures in protein dynamics.PLoS computational biology · 2022Article
- Advances in the Study of Bacterial Toxins, Their Roles and Mechanisms in Pathogenesis.The Malaysian journal of medical sciences : MJMS · 2022Review
- Effects of Chronic Photobiomodulation with Transcranial Near-Infrared Laser on Brain Metabolomics of Young and Aged Rats.Molecular neurobiology · 2021Article
- Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation.ACS omega · 2020Review
- How Ricin Damages the Ribosome.Toxins · 2019Review
- Translation in Prokaryotes.Cold Spring Harbor perspectives in biology · 2018Review
- RNA Structural Dynamics As Captured by Molecular Simulations: A Comprehensive Overview.Chemical reviews · 2018Review
- EF-Tu and EF-G are activated by allosteric effects.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Specific Substates of Ras To Interact with GAPs and Effectors: Revealed by Theoretical Simulations and FTIR Experiments.The journal of physical chemistry letters · 2018Article
- Precise quantification of translation inhibition by mRNA structures that overlap with the ribosomal footprint in N-terminal coding sequences.Nucleic acids research · 2017Article
- Article
- The GTPase hGBP1 converts GTP to GMP in two stepsChemical science · 2017Article
- Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome.Scientific reports · 2015Article
- A conserved histidine in switch-II of EF-G moderates release of inorganic phosphate.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several of the steps in protein synthesis on the ribosome utilize hydrolysis of guanosine triphosphate (GTP) as the driving force. This reaction is catalyzed by translation factors that become activated upon binding to the ribosome. The recently determined crystal structure of an elongation factor-Tu ternary complex bound to the ribosome allows the energetics of GTP activation to be explored by computer simulations. A central problem regards the role of the universally conserved histidine, which has been proposed to act as a general base for guanosine triphosphate hydrolysis. Here we report a detailed energetic and structural analysis of different possible protonation states that could be involved in activation of the reaction. We show that the histidine cannot act as a general base, but must be protonated and in its active conformation to promote GTP hydrolysis. We further show that the sarcin-ricin loop of the ribosome spontaneously drives the histidine into the correct conformation for GTP activation.
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