Evidence map›Paper›PMID 26367249›Full record

ArticleNature structural & molecular biology2015

Structure of a prokaryotic fumarate transporter reveals the architecture of the SLC26 family.

Eric R Geertsma, Yung-Ning Chang, Farooque R Shaik, Yvonne Neldner, Els Pardon, Jan Steyaert, Raimund Dutzler

Erratum issuedAbstract read
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In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 101 papers.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed
17.3field-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

101 citing papers in PubMed, 182 citations in OpenAlex.

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  17. SLC26 Anion Transporters.Handbook of experimental pharmacology · 2024
    Review
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41 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 3 countries.

Eric R GeertsmaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Yung-Ning ChangDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Farooque R ShaikDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Yvonne NeldnerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Els PardonStructural Biology Research Center, Vlaams Instituut voor Biotechnologie, Brussels, Belgium.ORCID http://orcid.org/0000-0002-2466-0172
Jan SteyaertStructural Biology Research Center, Vlaams Instituut voor Biotechnologie, Brussels, Belgium.
Raimund DutzlerDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
University of Zurich · CHGoethe University Frankfurt · DEVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SLC26 family of membrane proteins combines a variety of functions within a conserved molecular scaffold. Its members, besides coupled anion transporters and channels, include the motor protein Prestin, which confers electromotility to cochlear outer hair cells. To gain insight into the architecture of this protein family, we characterized the structure and function of SLC26Dg, a facilitator of proton-coupled fumarate symport, from the bacterium Deinococcus geothermalis. Its modular structure combines a transmembrane unit and a cytoplasmic STAS domain. The membrane-inserted domain consists of two intertwined inverted repeats of seven transmembrane segments each and resembles the fold of the unrelated transporter UraA. It shows an inward-facing, ligand-free conformation with a potential substrate-binding site at the interface between two helix termini at the center of the membrane. This structure defines the common framework for the diverse functional behavior of the SLC26 family.

Indexed as

Models, MolecularAnion Transport ProteinsBase SequenceChromatography, GelCloning, MolecularCrystallography, X-RayDeinococcusDNA PrimersElectrophoresis, Polyacrylamide GelEscherichia coliFluorescenceFumaratesMolecular Sequence DataMultigene FamilyOpen Reading FramesPolymerase Chain ReactionAnion Transport ProteinsDNA PrimersFumaratesSelenomethionine

Identifiers

PMID26367249
OpenAlexW2216424246

What OpenQuestion holds

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Registered trials

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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.