Evidence map›Paper›PMID 22163011›Full record

ArticlePloS one2011

AcrB trimer stability and efflux activity, insight from mutagenesis studies.

Linliang Yu, Wei Lu, Yinan Wei

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
  2. Review
  3. Structural analysis of resistance-nodulation cell division transporters.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  4. Review
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  7. Article
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  9. Article
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  14. Article
  15. Unfolding study of a trimeric membrane protein AcrB.Protein science : a publication of the Protein Society · 2014
    Article
  16. Article
  17. Assembling of AcrB trimer in cell membrane.Journal of molecular biology · 2012
    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

3 authors at 1 institution in 1 country.

Linliang YuDepartment of Chemistry, University of Kentucky, Lexington, Kentucky, United States of America.
Wei Lu
Yinan Wei
University of Kentucky · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The multidrug transporter AcrB in Escherichia coli exists and functions as a homo-trimer. The assembly process of obligate membrane protein oligomers, including AcrB, remains poorly understood. In a previous study, we have shown that individual AcrB subunit is capable of folding independently, suggesting that trimerization of AcrB follows a three-stage pathway in which monomers first fold, and then assemble. Here we destabilized the AcrB trimer through mutating a single Pro (P223) in the protruding loop of AcrB, which drastically reduced the protein activity. We replaced P223 separately with five residues, including Ala, Val, Tyr, Asn, and Gly, and found that AcrB(P223G) was the least active. Detailed characterization of AcrB(P223G) revealed that the protein existed as a well-folded monomer after purification, but formed a trimer in vivo. The function of the mutant could be partly restored through strengthening the stability of the trimer using an inter-subunit disulfide bond. Our results also suggested that the protruding loop is well structured during AcrB assembly with P223 served as a "wedge" close to the tip to stabilize the AcrB trimer structure. When this wedge is disrupted, the stability of the trimer is reduced, accompanied by a decrease of drug efflux activity.

Indexed as

Amino Acid SequenceATP-Binding Cassette, Sub-Family C ProteinsCircular DichroismCrystallography, X-RayDimerizationDisulfidesElectrophoresis, Polyacrylamide GelEscherichia coliEscherichia coli ProteinsMolecular Sequence DataMutagenesisMutagenesis, Site-DirectedMutationPlasmidsProtein Structure, QuaternaryProtein Structure, TertiaryAcrB protein, E coliATP-Binding Cassette, Sub-Family C ProteinsDisulfidesEscherichia coli ProteinsTrypsin

Identifiers

PMID22163011
PMCPMC3230630
OpenAlexW2028787442

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.