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Record W2314380047 · doi:10.11145/cb.v3i1.631

Domain Configuration Defines the Thermodynamic Landscape of Elongation Factor Tu Nucleotide Binding

2016· article· en· W2314380047 on OpenAlexaff
Dylan Girodat, Evan Mercier, Katehrine Gzyl, Hans‐Joachim Wieden

Bibliographic record

VenueBiomath Communications · 2016
Typearticle
Languageen
FieldBiochemistry, Genetics and Molecular Biology
TopicRNA and protein synthesis mechanisms
Canadian institutionsUniversity of Lethbridge
Fundersnot available
KeywordsGTP'EF-TuNucleotideElongation factorChemistryRibosomeTransfer RNABiophysicsRNABiologyBiochemistryEnzyme

Abstract

fetched live from OpenAlex

During protein synthesis Elongation Factor (EF) Tu plays a critical role in maintaining translational fidelity. EF-Tu functions as a molecular switch gating, in a nucleotide-dependent manner, the entrance of aminoacyl (aa)-tRNA into the translating ribosome. Correct codon-anticodon interaction stimulates EF-Tu to hydrolyze GTP to GDP and P i which is followed by a conformational change releasing the bound aa-tRNA. To prevent premature nucleotide exchange on the ribosome EF-Tu has evolved a 60-fold higher affinity for GDP than GTP (1). To this end we investigate what thermodynamic and structural features of EF-Tu give rise to these differences in nucleotide affinity, investigating how this property of EF-Tu contributes to translational fidelity.            Here we report a rapid kinetics analysis using the stopped-flow technique to measure the temperature dependence of the rate constants describing nucleotide association and dissociation. This has allowed us to determine the thermodynamic parameters governing these processes. We find that EF-Tu’s affinity to GTP and GDP differ mainly due differences in the transition state energy barriers of dissociation and not association. In addition, we observe that formation of the EF-Tu•GDP complex is enthalpically favored while the EF-Tu•GTP complex is entropically favored. This is consistent with our previous work reporting that the GTP dissociation is entropically driven (2). To provide a structural interpretation of the different thermodynamic contributions to nucleotide binding, we utilized Molecular Dynamic simulations of EF-Tu in its respective nucleotide bound forms. From these simulations we have identified a highly dynamic and transient hydrogen-bonding network that spans all domains of EF-Tu as the likely contributor to stabilizing the GDP conformation, whereas differences in water coordination defined by domain arrangement favor the GTP conformation. Our findings show that EF-Tu has evolutionarily modulated both the entropic and enthalpic contributions to the transition state barrier of nucleotide dissociation by modulating domain configuration in order for the fine-tuning of nucleotide-binding affinities. (1) Kiril B. Gromadzki, Hans-Joachim Wieden, and Marina V. Rodnina. Kinetic mechanism of Elongation Factor Ts-Catalyzed nucleotide exchange in Elongation Factor Tu. Biochemistry 41 , 162-169 (2002). (2) Evan Mercier, Dylan Girodat, Hans-Joachim Wieden. A conserved P-loop anchor limits the structural dynamics that mediate nucleotide dissociation in EF-Tu. Scientific Reports 5 , 1-9 (2015).

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

How this classification was reachedexpand

Full frame distilled prediction

Teacher imitation

Not calibrated prevalence, not ground truth. Human validation pending. Learned from the 10,348 direct Codex labels and 10,348 direct Gemma labels. Candidate is the union of thresholded teacher heads; consensus is their intersection. These outputs are machine_predicted_unvalidated and are not human labels or direct frontier model labels.

metaresearch head score (Codex)0.000
metaresearch head score (Gemma)0.000
Version: codex-gemma-dda1882f352aValidation status: machine_predicted_unvalidated
Candidate categoriesnone
Consensus categoriesnone
DomainCandidate signal: none · Consensus signal: none
Study designCandidate signal: Bench or experimental · Consensus signal: Bench or experimental
GenreCandidate signal: Empirical · Consensus signal: Empirical
Teacher disagreement score0.017
Threshold uncertainty score0.198

Codex and Gemma teacher scores by category

CategoryCodexGemma
Metaresearch0.0000.000
Meta-epidemiology (narrow)0.0000.000
Meta-epidemiology (broad)0.0000.000
Bibliometrics0.0000.000
Science and technology studies0.0000.000
Scholarly communication0.0000.000
Open science0.0010.000
Research integrity0.0000.000
Insufficient payload (model declined to judge)0.0000.000

Machine scores (provisional)

The two teacher heads of the student model, read on this work. A score orders the frame for review; it never asserts a category, and the validation status ships verbatim with every row.

Baseline scores from an immature model (maturity gate not passed, 7 training rounds). Scores rank; they never assert a category.

Opus teacher head0.021
GPT teacher head0.256
Teacher spread0.236 · how far apart the two teachers sit on this one work
Validation statusscore_only:v0-immature-baseline · verbatim from the scoring run: score_only means the number may rank works, and no category label ships from it

Classification

machine, unvalidated

Machine predicted; a candidate call from one teacher head, not a consensus.

The models applied no category: nothing in the taxonomy fit this work.
Study designBench or experimental
Domainnot available
GenreEmpirical

How this classification was reached, model by model and score by score, is at the end of the page under "How this classification was reached".

Quick stats

Citations0
Published2016
Admission routes1
Has abstractyes

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