Evidence map›Paper›PMID 16675957›Full record

ArticleThe EMBO journal2006

Escherichia coli acid resistance: pH-sensing, activation by chloride and autoinhibition in GadB.

Heinz Gut, Eugenia Pennacchietti, Robert A John, Francesco Bossa, Guido Capitani, Daniela De Biase, Markus G Grütter

Open access · greenAbstract read
In one paragraph

Article in The EMBO journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.0field-weighted citation impact, top 11% 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

42 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. A large-scale evolutionary and structural analysis of CLC channels and transporters.Protein science : a publication of the Protein Society · 2025
    Article
  3. Article
  4. Multitier regulation of theJournal of bacteriology · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Structural basis for substrate specificity of l-methionine decarboxylase.Protein science : a publication of the Protein Society · 2021
    Article
  12. Molecular Analysis of Glutamate Decarboxylases inFrontiers in microbiology · 2021
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

7 authors at 3 institutions in 3 countries.

Heinz GutBiochemisches Institut der Universität Zürich, Zürich, Switzerland.
Eugenia Pennacchietti
Robert A John
Francesco Bossa
Guido Capitani
Daniela De Biase
Markus G Grütter
Sapienza University of Rome · ITUniversity of Zurich · CHCardiff University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Escherichia coli and other enterobacteria exploit the H+ -consuming reaction catalysed by glutamate decarboxylase to survive the stomach acidity before reaching the intestine. Here we show that chloride, extremely abundant in gastric secretions, is an allosteric activator producing a 10-fold increase in the decarboxylase activity at pH 5.6. Cooperativity and sensitivity to chloride were lost when the N-terminal 14 residues, involved in the formation of two triple-helix bundles, were deleted by mutagenesis. X-ray structures, obtained in the presence of the substrate analogue acetate, identified halide-binding sites at the base of each N-terminal helix, showed how halide binding is responsible for bundle stability and demonstrated that the interconversion between active and inactive forms of the enzyme is a stepwise process. We also discovered an entirely novel structure of the cofactor pyridoxal 5'-phosphate (aldamine) to be responsible for the reversibly inactivated enzyme. Our results link the entry of chloride ions, via the H+/Cl- exchange activities of ClC-ec1, to the trigger of the acid stress response in the cell when the intracellular proton concentration has not yet reached fatal values.

Indexed as

Hydrogen-Ion ConcentrationAcidsAllosteric RegulationAntiportersChloridesCrystallography, X-RayEnzyme ActivationEnzyme StabilityEscherichia coliEscherichia coli ProteinsGlutamate DecarboxylaseHumansMembrane ProteinsModels, MolecularProtein ConformationAcidsAntiportersChloridesEscherichia coli ProteinsGlutamate DecarboxylaseMembrane Proteins

Identifiers

PMID16675957
PMCPMC1478166
OpenAlexW1984134434

What OpenQuestion holds

Textmetadata
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.