Evidence map›Paper›PMID 22178925›Full record

ArticleNature2011

Antiparallel EmrE exports drugs by exchanging between asymmetric structures.

Emma A Morrison, Gregory T DeKoster, Supratik Dutta, Reza Vafabakhsh, Michael W Clarkson, Arjun Bahl, Dorothee Kern, Taekjip Ha, Katherine A Henzler-Wildman

Abstract read
In one paragraph

Article in Nature, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.

0numbers the graph read from it
0cells of the map it votes in
122citing papers in PubMed
9.0field-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

122 citing papers in PubMed, 224 citations in OpenAlex.

  1. Article
  2. Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Backbone and sidechainBiomolecular NMR assignments · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Solid-State NMR of Virus Membrane Proteins.Accounts of chemical research · 2025
    Article
  13. Article
  14. Article
  15. Structural analysis of resistance-nodulation cell division transporters.Microbiology and molecular biology reviews : MMBR · 2024
    Review
  16. Peripheral positions encode transport specificity in the small multidrug resistance exporters.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  17. Article
  18. A Small Multidrug Resistance Transporter inbioRxiv : the preprint server for biology · 2024
    Article
  19. Article
  20. Article

62 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

9 authors at 3 institutions in 1 country.

Emma A MorrisonDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Gregory T DeKoster
Supratik Dutta
Reza Vafabakhsh
Michael W Clarkson
Arjun Bahl
Dorothee Kern
Taekjip Ha
Katherine A Henzler-Wildman
Washington University in St. Louis · USBrandeis University · USUniversity of Illinois Urbana-Champaign · US

Funding

TRANSPORT MECHANISM OF THE MULTIDRUG RESISTANCE EFFLUX PROTEIN, EMRER01GM095839 · NIGMS · WASHINGTON UNIVERSITY · PI HENZLER-WILDMAN, KATHERINE ANNE · 2011 to 2020
$3.1M
Howard Hughes Medical InstituteNIGMS NIH HHS 1R01GM095839NIGMS NIH HHS R01 GM095839
6 · The paper itself

Abstract

Small multidrug resistance transporters provide an ideal system to study the minimal requirements for active transport. EmrE is one such transporter in Escherichia coli. It exports a broad class of polyaromatic cation substrates, thus conferring resistance to drug compounds matching this chemical description. However, a great deal of controversy has surrounded the topology of the EmrE homodimer. Here we show that asymmetric antiparallel EmrE exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane. We quantitatively measure the global conformational exchange between these two states for substrate-bound EmrE in bicelles using solution NMR dynamics experiments. Förster resonance energy transfer reveals that the monomers within each dimer are antiparallel, and paramagnetic relaxation enhancement NMR experiments demonstrate differential water accessibility of the two monomers within each dimer. Our experiments reveal a 'dynamic symmetry' that reconciles the asymmetric EmrE structure with the functional symmetry of residues in the active site.

Indexed as

AntiportersBiological TransportCatalytic DomainEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferModels, MolecularNuclear Magnetic Resonance, BiomolecularPharmaceutical PreparationsProtein ConformationProtein MultimerizationWaterAntiportersEmrE protein, E coliEscherichia coli ProteinsPharmaceutical PreparationsWater

Identifiers

PMID22178925
PMCPMC3253143
OpenAlexW2017898428

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.