ArticleThe Journal of biological chemistry2016
Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Interplay between Inter-Subunit Rotation of the Ribosome and Binding of Translational GTPases.International journal of molecular sciences · 2023Article
- In silico analysis of bacterial translation factors reveal distinct translation event specific pI values.BMC genomics · 2021Article
- Translational GTPase BipA Is Involved in the Maturation of a Large Subunit of Bacterial Ribosome at Suboptimal Temperature.Frontiers in microbiology · 2021Article
- Ribosome assembly defects subvert initiation Factor3 mediated scrutiny of bona fide start signal.Nucleic acids research · 2019Article
- The GTPase BipA expressed at low temperature inThe Journal of biological chemistry · 2018Article
- Translation Elongation Factor 4 (LepA) Contributes to Tetracycline Susceptibility by Stalling Elongating Ribosomes.Antimicrobial agents and chemotherapy · 2018Article
- Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.Molecular and cellular biology · 2017Review
- Conserved GTPase LepA (Elongation Factor 4) functions in biogenesis of the 30S subunit of the 70S ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Similarity and diversity of translational GTPase factors EF-G, EF4, and BipA: From structure to function.RNA biology · 2016Review
- EF4 reveals the energy barrier for tRNA back-translocation in the peptidyl transferase center.RNA biology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.