Evidence map›Paper›PMID 25023443›Full record

ArticleNature communications2014

Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na+ coupling.

Camilo Perez, Belinda Faust, Ahmad Reza Mehdipour, Kevin A Francesconi, Lucy R Forrest, Christine Ziegler

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  4. Review
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  7. MolDy: molecular dynamics simulation made easy.Bioinformatics (Oxford, England) · 2024
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  8. Identification of the potassium-binding site in serotonin transporter.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Review
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  13. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Kinetic Models of Secondary Active Transporters.International journal of molecular sciences · 2019
    Article
  18. Article
  19. Interrogating the conformational dynamics of BetP transport.The Journal of general physiology · 2019
    Article
  20. 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

6 authors at 3 institutions in 2 countries.

Camilo Perez1] Structural Biology Department, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany [2] [3].
Belinda Faust1] Structural Biology Department, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany [2] [3].
Ahmad Reza Mehdipour1] Computational Structural Biology Group, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany [2].
Kevin A FrancesconiInstitute of Chemistry-Analytical Chemistry, University of Graz, Graz 8010, Austria.
Lucy R Forrest1] Computational Structural Biology Group, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany [2].
Christine Ziegler1] Structural Biology Department, Max-Planck Institute of Biophysics, Frankfurt am Main 60438, Germany [2] Institute of Biophysics and Biophysical Chemistry, University of Regensburg, Regensburg 95053, Germany.
Max Planck Institute of Biophysics · DEUniversity of Graz · ATUniversity of Regensburg · DE

Funding

Computational Studies of Membrane Transport ProteinsZIANS003139 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI FORREST, LUCY · 2014 to 2025
$13.7M
Intramural NIH HHS Z99 NS999999Wellcome Trust 092809
6 · The paper itself

Abstract

The Na(+)-coupled betaine symporter BetP shares a highly conserved fold with other sequence unrelated secondary transporters, for example, with neurotransmitter symporters. Recently, we obtained atomic structures of BetP in distinct conformational states, which elucidated parts of its alternating-access mechanism. Here, we report a structure of BetP in a new outward-open state in complex with an anomalous scattering substrate, adding a fundamental piece to an unprecedented set of structural snapshots for a secondary transporter. In combination with molecular dynamics simulations these structural data highlight important features of the sequential formation of the substrate and sodium-binding sites, in which coordinating water molecules play a crucial role. We observe a strictly interdependent binding of betaine and sodium ions during the coupling process. All three sites undergo progressive reshaping and dehydration during the alternating-access cycle, with the most optimal coordination of all substrates found in the closed state.

Indexed as

Carrier ProteinsElectrophysiologyEscherichia coliGABA Plasma Membrane Transport ProteinsMolecular Dynamics SimulationMutagenesis, Site-DirectedSodiumbetaine plasma membrane transport proteinsCarrier ProteinsGABA Plasma Membrane Transport ProteinsSodium

Identifiers

PMID25023443
PMCPMC4745115
OpenAlexW2039042916

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.