Evidence map›Paper›PMID 29109439›Full record

ArticleNature communications2017

Crystal structure of tripartite-type ABC transporter MacB from Acinetobacter baumannii.

Ui Okada, Eiki Yamashita, Arthur Neuberger, Mayu Morimoto, Hendrik W van Veen, Satoshi Murakami

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.1field-weighted citation impact, top 3% 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

57 citing papers in PubMed, 103 citations in OpenAlex.

  1. Article
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  7. Inside-out, antimicrobial resistance mediated by efflux pumps in clinical strains of Acinetobacter baumannii isolated from burn wound infections.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024
    Article
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  14. Review
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  20. ABC Transporters in Bacterial Nanomachineries.International journal of molecular sciences · 2023
    Review
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

6 authors at 3 institutions in 2 countries.

Ui OkadaDepartment of Life Science, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.ORCID http://orcid.org/0000-0001-7633-9308
Eiki YamashitaInstitute for Protein Research, Osaka University, Suita, Osaka, 565-0871, Japan.
Arthur NeubergerDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID http://orcid.org/0000-0002-7744-6559
Mayu MorimotoDepartment of Life Science, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.
Hendrik W van VeenDepartment of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, UK.ORCID http://orcid.org/0000-0002-9658-8077
Satoshi MurakamiDepartment of Life Science, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan. murakami@bio.titech.ac.jp.ORCID http://orcid.org/0000-0001-5553-7663
Tokyo Institute of Technology · JPUniversity of Cambridge · GBProtein Research Foundation · JP

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_PC_14116
6 · The paper itself

Abstract

The MacA-MacB-TolC tripartite complex is a transmembrane machine that spans both plasma membrane and outer membrane and actively extrudes substrates, including macrolide antibiotics, virulence factors, peptides and cell envelope precursors. These transport activities are driven by the ATPase MacB, a member of the ATP-binding cassette (ABC) superfamily. Here, we present the crystal structure of MacB at 3.4-Å resolution. MacB forms a dimer in which each protomer contains a nucleotide-binding domain and four transmembrane helices that protrude in the periplasm into a binding domain for interaction with the membrane fusion protein MacA. MacB represents an ABC transporter in pathogenic microorganisms with unique structural features.

Indexed as

Acinetobacter baumanniiAmino Acid SequenceATP-Binding Cassette TransportersBacterial ProteinsConserved SequenceCrystallography, X-RayDrug Resistance, Multiple, BacterialEscherichia coliModels, MolecularProtein DomainsProtein Structure, QuaternaryRecombinant ProteinsSequence Homology, Amino AcidATP-Binding Cassette TransportersBacterial ProteinsRecombinant Proteins

Identifiers

PMID29109439
PMCPMC5673888
OpenAlexW2766607130

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.