Evidence map›Paper›PMID 30387776›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

BpeB, a major resistance-nodulation-cell division transporter from Burkholderia cenocepacia: construct design, crystallization and preliminary structural analysis.

Tomonari Horikawa, Li Wei Hung, Heung Bok Kim, David Shaya, Chang Yub Kim, Thomas C Terwilliger, Eiki Yamashita, Maho Aoki, Ui Okada, Satoshi Murakami

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact, top 94% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Crystal structures of multidrug efflux transporters fromProceedings of the National Academy of Sciences of the United States of America · 2023
    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

10 authors at 3 institutions in 2 countries.

Tomonari HorikawaDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Li Wei HungLos Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0001-6690-8458
Heung Bok KimLos Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0002-4359-8423
David ShayaLos Alamos National Laboratory, Los Alamos, NM 87545, USA.
Chang Yub KimLos Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0001-9353-5909
Thomas C TerwilligerLos Alamos National Laboratory, Los Alamos, NM 87545, USA.ORCID 0000-0001-6384-0320
Eiki YamashitaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.ORCID 0000-0002-4278-0039
Maho AokiDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.
Ui OkadaDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.ORCID 0000-0001-7633-9308
Satoshi MurakamiDepartment of Life Science and Technology, Tokyo Institute of Technology, Yokohama 226-8501, Japan.ORCID 0000-0001-5553-7663
Los Alamos National Laboratory · USTokyo Institute of Technology · JPProtein Research Foundation · JP

Funding

Japan Society for the Promotion of Science 18H02386
6 · The paper itself

Abstract

Burkholderia cenocepacia is an opportunistic pathogen that infects cystic fibrosis patients, causing pneumonia and septicemia. B. cenocepacia has intrinsic antibiotic resistance against monobactams, aminoglycosides, chloramphenicol and fluoroquinolones that is contributed by a homologue of BpeB, which is a member of the resistance-nodulation-cell division (RND)-type multidrug-efflux transporters. Here, the cloning, overexpression, purification, construct design for crystallization and preliminary X-ray diffraction analysis of this BpeB homologue from B. cenocepacia are reported. Two truncation variants were designed to remove possible disordered regions based on comparative sequence and structural analysis to salvage the wild-type protein, which failed to crystallize. The 17-residue carboxyl-terminal truncation yielded crystals that diffracted to 3.6 Å resolution. The efflux function measured using minimal inhibitory concentration assays indicated that the truncation decreased, but did not eliminate, the efflux activity of the transporter.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsBurkholderia cenocepaciaCloning, MolecularCrystallizationCrystallography, X-RayDrug Resistance, Multiple, BacterialMembrane Transport ProteinsMicrobial Sensitivity TestsAnti-Bacterial AgentsBacterial ProteinsMembrane Transport ProteinsBurkholderiadrug exportermembrane transportermultidrug resistance

Identifiers

PMID30387776
PMCPMC6213979
OpenAlexW2895923657

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.