Evidence map›Paper›PMID 33909410›Full record

ReviewChemical reviews2021

Structure, Assembly, and Function of Tripartite Efflux and Type 1 Secretion Systems in Gram-Negative Bacteria.

Ilyas Alav, Jessica Kobylka, Miriam S Kuth, Klaas M Pos, Martin Picard, Jessica M A Blair, Vassiliy N Bavro

Open access · hybridAbstract readReview
In one paragraph

Review in Chemical reviews, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 133 papers.

0numbers the graph read from it
0cells of the map it votes in
133citing papers in PubMed
12.5field-weighted citation impact, top 1% 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

133 citing papers in PubMed, 226 citations in OpenAlex.

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  14. Genomic Characterization ofPlants (Basel, Switzerland) · 2026
    Article
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73 more citing papers are in PubMed but not listed here.

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 4 institutions in 3 countries.

Ilyas AlavInstitute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.
Jessica KobylkaInstitute of Biochemistry, Biocenter, Goethe Universität Frankfurt, Max-von-Laue-Straße 9, D-60438 Frankfurt, Germany.
Miriam S KuthInstitute of Biochemistry, Biocenter, Goethe Universität Frankfurt, Max-von-Laue-Straße 9, D-60438 Frankfurt, Germany.
Klaas M PosInstitute of Biochemistry, Biocenter, Goethe Universität Frankfurt, Max-von-Laue-Straße 9, D-60438 Frankfurt, Germany.
Martin PicardLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, CNRS UMR 7099, Université de Paris, 75005 Paris, France.ORCID 0000-0002-6518-8900
Jessica M A BlairInstitute of Microbiology and Infection, College of Medical and Dental Sciences, University of Birmingham, Edgbaston, Birmingham B15 2TT, United Kingdom.ORCID 0000-0001-6904-4253
Vassiliy N BavroSchool of Life Sciences, University of Essex, Colchester, CO4 3SQ United Kingdom.ORCID 0000-0003-2330-8924
Goethe University Frankfurt · DEUniversity of Birmingham · GBCentre National de la Recherche Scientifique · FRUniversity of Essex · GB

Funding

Resource for Biocomputing Visualization and InformaticsP41GM103311 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2012 to 2017
$8.2M
Biotechnology and Biological Sciences Research Council BB/M01116X/1Biotechnology and Biological Sciences Research Council BB/M02623X/1Biotechnology and Biological Sciences Research Council BB/N002776/1NIGMS NIH HHS P41 GM103311
6 · The paper itself

Abstract

Tripartite efflux pumps and the related type 1 secretion systems (T1SSs) in Gram-negative organisms are diverse in function, energization, and structural organization. They form continuous conduits spanning both the inner and the outer membrane and are composed of three principal components-the energized inner membrane transporters (belonging to ABC, RND, and MFS families), the outer membrane factor channel-like proteins, and linking the two, the periplasmic adaptor proteins (PAPs), also known as the membrane fusion proteins (MFPs). In this review we summarize the recent advances in understanding of structural biology, function, and regulation of these systems, highlighting the previously undescribed role of PAPs in providing a common architectural scaffold across diverse families of transporters. Despite being built from a limited number of basic structural domains, these complexes present a staggering variety of architectures. While key insights have been derived from the RND transporter systems, a closer inspection of the operation and structural organization of different tripartite systems reveals unexpected analogies between them, including those formed around MFS- and ATP-driven transporters, suggesting that they operate around basic common principles. Based on that we are proposing a new integrated model of PAP-mediated communication within the conformational cycling of tripartite systems, which could be expanded to other types of assemblies.

Indexed as

ATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsGram-Negative BacteriaMembrane Transport ProteinsMolecular Dynamics SimulationProtein ConformationStructure-Activity RelationshipType I Secretion SystemsATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsMembrane Transport ProteinsType I Secretion Systems

Identifiers

PMID33909410
PMCPMC8277102
OpenAlexW3158875798

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.