Evidence map›Paper›PMID 26775572›Full record

ArticleArchives of biochemistry and biophysics2016

Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.

Chao Zhao, Hiba Syed, Sherif S Hassan, Vineet K Singh, Zulfiqar Ahmad

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Archives of biochemistry and biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Safranal and its analogs inhibit Escherichia coli ATP synthase and cell growth.International journal of biological macromolecules · 2017
    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

5 authors at 2 institutions in 2 countries.

Chao ZhaoDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA.
Hiba SyedDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA.
Sherif S HassanDepartment of Anatomy, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA; Faculty of Medicine, Cairo University, Cairo, Egypt.
Vineet K SinghDepartment of Microbiology & Immunology, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA.
Zulfiqar AhmadDepartment of Biochemistry, Kirksville College of Osteopathic Medicine, A.T. Still University, Kirksville, MO, 63501, USA. Electronic address: zahmad@atsu.edu.
A.T. Still University · USCairo University · EG

Funding

Molecular Modulation of Catalytic Sites of Escherichia coli F1Fo ATP SynthaseR15GM085771 · NIGMS · EAST TENNESSEE STATE UNIVERSITY · PI AHMAD, ZULFIQAR · 2009 to 2009
$209k
NIGMS NIH HHS GM085771NIGMS NIH HHS R15 GM085771
6 · The paper itself

Abstract

We studied the functional role of highly conserved VISIT-DG sequence residues αIle-346 and αIle-348 in the catalytic sites of Escherichia coli F1Fo ATP synthase. αIle-346 is in close proximity, 2.98 and 3.63 Å, to the two known phosphate binding residues αR376 and βR182; αIle-348 is situated within 3.66 Å from βR182. Single or double mutants of both αI346 and αI348 resulted in a variable loss of oxidative phosphorylation and ATPase activity. Azide, fluoroaluminate, and fluoroscandium caused insignificant to significant inhibition of mutants. Whereas the wild-type enzyme was completely inhibited by NBD-Cl (7-chloro-4-nitrobenzo-2-oxa-1, 3-diazole), a variable extent of inhibition was observed for αI346 and αI348 mutants. MgPi protection against NBD-Cl induced inhibition of wild-type, αI346, and αI348 demonstrated that, although strongly conserved, αI346 and αI348 have no direct role in phosphate binding. Insertion of Arginine in the form of αI346R/βR182A, αI346R/αR376A, or αI348R/βR182A was able to compensate for the absence of known phosphate-binding Arginine residues βR182 and αR376. Results also suggest that αIle-346 and αIle-348 seem to have functional importance in upholding the phosphate-binding subdomain and transition state stabilization in the catalytic sites of E. coli ATP synthase.

Indexed as

Binding SitesCatalysisEnzyme ActivationEscherichia coliPhosphatesProtein BindingProton-Translocating ATPasesStructure-Activity RelationshipSubstrate SpecificityPhosphatesProton-Translocating ATPasesATPase inhibitionEscherichia coli ATP synthaseF(1)F(o) ATP synthaseOxidative phosphorylationPi binding residues

Identifiers

PMID26775572
PMCPMC5884630
OpenAlexW2238723152

What OpenQuestion holds

Textmetadata
LicenceTDM
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.