Evidence map›Paper›PMID 26264741›Full record

ArticleScientific reports2015

A conserved histidine in switch-II of EF-G moderates release of inorganic phosphate.

Ravi Kiran Koripella, Mikael Holm, Daniel Dourado, Chandra Sekhar Mandava, Samuel Flores, Suparna Sanyal

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
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  9. Selective translation by alternative bacterial ribosomes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Complementary charge-based interaction between the ribosomal-stalk protein L7/12 and IF2 is the key to rapid subunit association.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  15. Article
  16. Structural insights into ribosome translocation.Wiley interdisciplinary reviews. RNA · 2016
    Review
  17. EF-G Activation by Phosphate Analogs.Journal of molecular biology · 2016
    Article
  18. Article
  19. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Ravi Kiran KoripellaDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Mikael HolmDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Daniel DouradoDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Chandra Sekhar MandavaDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Samuel FloresDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Suparna SanyalDepartment of Cell and Molecular Biology, Uppsala University, Box-596, BMC, 75124, Uppsala, Sweden.
Uppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Elongation factor G (EF-G), a translational GTPase responsible for tRNA-mRNA translocation possesses a conserved histidine (H91 in Escherichia coli) at the apex of switch-II, which has been implicated in GTPase activation and GTP hydrolysis. While H91A, H91R and H91E mutants showed different degrees of defect in ribosome associated GTP hydrolysis, H91Q behaved like the WT. However, all these mutants, including H91Q, are much more defective in inorganic phosphate (Pi) release, thereby suggesting that H91 facilitates Pi release. In crystal structures of the ribosome bound EF-G•GTP a tight coupling between H91 and the γ-phosphate of GTP can be seen. Following GTP hydrolysis, H91 flips ~140° in the opposite direction, probably with Pi still coupled to it. This, we suggest, promotes Pi to detach from GDP and reach the inter-domain space of EF-G, which constitutes an exit path for the Pi. Molecular dynamics simulations are consistent with this hypothesis and demonstrate a vital role of an Mg(2+) ion in the process.

Indexed as

Conserved SequenceAmino Acid SequenceGuanosine TriphosphateHistidineHydrolysisMolecular Dynamics SimulationMolecular Sequence DataPeptide Elongation Factor GPhosphatesSequence Homology, Amino AcidGuanosine TriphosphateHistidinePeptide Elongation Factor GPhosphates

Identifiers

PMID26264741
PMCPMC4532990
OpenAlexW2146901272

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.