Evidence map›Paper›PMID 25271373›Full record

ArticleeLife2014

Allosteric signalling in the outer membrane translocation domain of PapC usher.

Irene Farabella, Thieng Pham, Nadine S Henderson, Sebastian Geibel, Gilles Phan, David G Thanassi, Anne H Delcour, Gabriel Waksman, Maya Topf

Erratum issuedAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Self-organization, entropy and allostery.Biochemical Society transactions · 2018
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Irene FarabellaInstitute of Structural and Molecular Biology, Birkbeck College and University College London, London, United Kingdom.
Thieng PhamDepartment of Biology and Biochemistry, University of Houston, Houston, United States.
Nadine S HendersonDepartment of Molecular Genetics and Microbiology, Center for Infectious Diseases, Stony Brook University, Stony Brook, United States.
Sebastian GeibelInstitute of Structural and Molecular Biology, Birkbeck College and University College London, London, United Kingdom.
Gilles PhanInstitute of Structural and Molecular Biology, Birkbeck College and University College London, London, United Kingdom.
David G ThanassiDepartment of Molecular Genetics and Microbiology, Center for Infectious Diseases, Stony Brook University, Stony Brook, United States.
Anne H DelcourDepartment of Biology and Biochemistry, University of Houston, Houston, United States.
Gabriel WaksmanInstitute of Structural and Molecular Biology, Birkbeck College and University College London, London, United Kingdom.
Maya TopfInstitute of Structural and Molecular Biology, Birkbeck College and University College London, London, United Kingdom.

Funding

Mechanism of the Usher in Assembly and Secretion of PiliR01GM062987 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI David G Thanassi · 2001 to 2026
$7.7M
Biotechnology and Biological Sciences Research Council BB/K01692X/1Medical Research Council 018434Medical Research Council G0600084NIGMS NIH HHS GM062987NIGMS NIH HHS R01 GM062987Wellcome TrustWellcome Trust 086711/z/08/z
6 · The paper itself

Abstract

PapC ushers are outer-membrane proteins enabling assembly and secretion of P pili in uropathogenic E. coli. Their translocation domain is a large β-barrel occluded by a plug domain, which is displaced to allow the translocation of pilus subunits across the membrane. Previous studies suggested that this gating mechanism is controlled by a β-hairpin and an α-helix. To investigate the role of these elements in allosteric signal communication, we developed a method combining evolutionary and molecular dynamics studies of the native translocation domain and mutants lacking the β-hairpin and/or the α-helix. Analysis of a hybrid residue interaction network suggests distinct regions (residue 'communities') within the translocation domain (especially around β12-β14) linking these elements, thereby modulating PapC gating. Antibiotic sensitivity and electrophysiology experiments on a set of alanine-substitution mutants confirmed functional roles for four of these communities. This study illuminates the gating mechanism of PapC ushers and its importance in maintaining outer-membrane permeability.

Indexed as

AlanineAllosteric RegulationAmino Acid MotifsAmino Acid SubstitutionAnti-Bacterial AgentsCell Membrane PermeabilityErythromycinEscherichia coli ProteinsFimbriae, BacterialGene ExpressionMembrane PotentialsMolecular Dynamics SimulationMolecular Sequence DataMutationPorinsProtein Structure, SecondaryAlanineAnti-Bacterial AgentsatpG protein, E coliErythromycinEscherichia coli ProteinsPorinsProtein SubunitsVancomycinbiophysicsdynamicsE. colievolutionouter membrane proteinstructural biologystructure

Identifiers

PMID25271373
PMCPMC4356140

What OpenQuestion holds

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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.