Evidence map›Paper›PMID 26018081›Full record

ArticleThe Journal of biological chemistry2015

Histidine 114 Is Critical for ATP Hydrolysis by the Universally Conserved ATPase YchF.

Kirsten S Rosler, Evan Mercier, Ian C Andrews, Hans-Joachim Wieden

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Construction and Use of TransposonFrontiers in microbiology · 2019
    Article
  9. 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

4 authors.

Kirsten S RoslerFrom the Department of Chemistry and Biochemistry, Alberta RNA Research and Training Institute, University of Lethbridge, Lethbridge, Alberta T1K 3M4, Canada.
Evan MercierFrom the Department of Chemistry and Biochemistry, Alberta RNA Research and Training Institute, University of Lethbridge, Lethbridge, Alberta T1K 3M4, Canada.
Ian C AndrewsFrom the Department of Chemistry and Biochemistry, Alberta RNA Research and Training Institute, University of Lethbridge, Lethbridge, Alberta T1K 3M4, Canada.
Hans-Joachim WiedenFrom the Department of Chemistry and Biochemistry, Alberta RNA Research and Training Institute, University of Lethbridge, Lethbridge, Alberta T1K 3M4, Canada hj.wieden@uleth.ca.

Funding

Canadian Institutes of Health Research MOP103033Canadian Institutes of Health Research MOP114938Canadian Institutes of Health Research MOP84917Canadian Institutes of Health Research MOP89353
6 · The paper itself

Abstract

GTPases perform a wide range of functions, ranging from protein synthesis to cell signaling. Of all known GTPases, only eight are conserved across all three domains of life. YchF is one of these eight universally conserved GTPases; however, its cellular function and enzymatic properties are poorly understood. YchF differs from the classical GTPases in that it has a higher affinity for ATP than for GTP and is a functional ATPase. As a hydrophobic amino acid-substituted ATPase, YchF does not possess the canonical catalytic Gln required for nucleotide hydrolysis. To elucidate the catalytic mechanism of ATP hydrolysis by YchF, we have taken a two-pronged approach combining classical biochemical and in silico techniques. The use of molecular dynamics simulations allowed us to complement our biochemical findings with information about the structural dynamics of YchF. We have thereby identified the highly conserved His-114 as critical for the ATPase activity of YchF from Escherichia coli. His-114 is located in a flexible loop of the G-domain, which undergoes nucleotide-dependent conformational changes. The use of a catalytic His is also observed in the hydrophobic amino acid-substituted GTPase RbgA and is an identifier of the translational GTPase family.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid MotifsCrystallography, X-RayEscherichia coliEscherichia coli ProteinsGTP PhosphohydrolasesHistidineHydrolysisKineticsMolecular Dynamics SimulationProtein BiosynthesisProtein ConformationRibosomesAdenosine TriphosphatasesAdenosine TriphosphateEscherichia coli ProteinsGTP PhosphohydrolasesHistidineYchF protein, E. coliATPasecatalytic mechanismconformational changeHAS-ATPasemolecular dynamicsmolecular switchnucleotide bindingpre-steady-state kineticsribosomeYchF

Identifiers

PMID26018081
PMCPMC4513122

What OpenQuestion holds

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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.