Evidence map›Paper›PMID 28504659›Full record

ArticleNature microbiology2017

Structure of the MacAB-TolC ABC-type tripartite multidrug efflux pump.

Anthony W P Fitzpatrick, Salomé Llabrés, Arthur Neuberger, James N Blaza, Xiao-Chen Bai, Ui Okada, Satoshi Murakami, Hendrik W van Veen, Ulrich Zachariae, Sjors H W Scheres and 2 more

Open access · greenAbstract read
In one paragraph

Article in Nature microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
6.7field-weighted citation impact, top 2% 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

113 citing papers in PubMed, 190 citations in OpenAlex.

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  16. Efflux-Mediated Resistance inAntibiotics (Basel, Switzerland) · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Article

53 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

12 authors at 5 institutions in 3 countries.

Anthony W P Fitzpatrick *Medical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, U.K.
Salomé LlabrésComputational Biology, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Arthur NeubergerDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, U.K.
James N BlazaMRC Mitochondrial Biology Unit, Cambridge Biomedical Campus, Hills Road, Cambridge, CB2 0XY.
Xiao-Chen BaiMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, U.K.
Ui OkadaDepartment of Life Science, Tokyo Institute of Technology, 4259-J2-17, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.
Satoshi MurakamiDepartment of Life Science, Tokyo Institute of Technology, 4259-J2-17, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.
Hendrik W van VeenDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge CB2 1PD, U.K.
Ulrich ZachariaeComputational Biology, School of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, U.K.
Sjors H W ScheresMedical Research Council Laboratory of Molecular Biology, Cambridge Biomedical Campus, Francis Crick Avenue, Cambridge CB2 0QH, U.K.
Ben F LuisiDepartment of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, U.K.
Dijun Du *Department of Biochemistry, University of Cambridge, Tennis Court Road, Cambridge CB2 1GA, U.K.
University of Cambridge · GBMRC Laboratory of Molecular Biology · GBTokyo Institute of Technology · JPUniversity of Dundee · GBMRC Mitochondrial Biology Unit · GB

Funding

Medical Research Council MC_PC_14116Medical Research Council MC_U105663141Medical Research Council MC_UP_A025_1013Wellcome Trust
6 · The paper itself

Abstract

The MacA-MacB-TolC assembly of Escherichia coli is a transmembrane machine that spans the cell envelope and actively extrudes substrates, including macrolide antibiotics and polypeptide virulence factors. These transport processes are energized by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. We present an electron cryo-microscopy structure of the ABC-type tripartite assembly at near-atomic resolution. A hexamer of the periplasmic protein MacA bridges between a TolC trimer in the outer membrane and a MacB dimer in the inner membrane, generating a quaternary structure with a central channel for substrate translocation. A gating ring found in MacA is proposed to act as a one-way valve in substrate transport. The MacB structure features an atypical transmembrane domain with a closely packed dimer interface and a periplasmic opening that is the likely portal for substrate entry from the periplasm, with subsequent displacement through an allosteric transport mechanism.

Indexed as

ATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsCryoelectron MicroscopyEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularProtein ConformationProtein MultimerizationATP-Binding Cassette TransportersBacterial Outer Membrane ProteinsEscherichia coli ProteinsMacAB protein, E coliMembrane Transport ProteinstolC protein, E coli

Identifiers

PMID28504659
PMCPMC5447821
OpenAlexW2614889529

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.