Evidence map›Paper›PMID 33350937›Full record

ArticleeLife2020

In vitro reconstitution of dynamically interacting integral membrane subunits of energy-coupling factor transporters.

Inda Setyawati, Weronika K Stanek, Maria Majsnerowska, Lotteke J Y M Swier, Els Pardon, Jan Steyaert, Albert Guskov, Dirk J Slotboom

Open access · goldAbstract read
In one paragraph

Article in eLife, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

13 citing papers in PubMed, 16 citations in OpenAlex.

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  13. Insights into the bilayer-mediated toppling mechanism of a folate-specific ECF transporter by cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

8 authors at 3 institutions in 4 countries.

Inda Setyawati *Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.
Weronika K Stanek *Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.ORCID 0000-0001-7846-3927
Maria Majsnerowska *Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.
Lotteke J Y M SwierGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.
Els PardonStructural Biology Brussels, Vrije Universiteit Brussel, VUB, Brussels, Belgium.ORCID 0000-0002-2466-0172
Jan SteyaertStructural Biology Brussels, Vrije Universiteit Brussel, VUB, Brussels, Belgium.ORCID 0000-0002-3825-874X
Albert GuskovGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.ORCID 0000-0003-2340-2216
Dirk J SlotboomGroningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, Netherlands.ORCID 0000-0002-5804-9689
University of Groningen · NLVrije Universiteit Brussel · BEMoscow Institute of Physics and Technology · RU

Funding

Horizon 2020 Grant 731005Instruct-ERIC PID 6357Nederlandse Organisatie voor Wetenschappelijk Onderzoek TOP grant 714.018.003
6 · The paper itself

Abstract

Energy-coupling factor (ECF) transporters mediate import of micronutrients in prokaryotes. They consist of an integral membrane S-component (that binds substrate) and ECF module (that powers transport by ATP hydrolysis). It has been proposed that different S-components compete for docking onto the same ECF module, but a minimal liposome-reconstituted system, required to substantiate this idea, is lacking. Here, we co-reconstituted ECF transporters for folate (ECF-FolT2) and pantothenate (ECF-PanT) into proteoliposomes, and assayed for crosstalk during active transport. The kinetics of transport showed that exchange of S-components is part of the transport mechanism. Competition experiments suggest much slower substrate association with FolT2 than with PanT. Comparison of a crystal structure of ECF-PanT with previously determined structures of ECF-FolT2 revealed larger conformational changes upon binding of folate than pantothenate, which could explain the kinetic differences. Our work shows that a minimal in vitro system with two reconstituted transporters recapitulates intricate kinetics behaviour observed in vivo.

Indexed as

ATP-Binding Cassette TransportersBiological Transport, ActiveIn Vitro TechniquesLactobacillus delbrueckiiModels, MolecularProtein BindingProtein ConformationATP-Binding Cassette TransportersABC transporterbiochemistrychemical biologyLactobacillus delbrueckiimembrane transportmolecular biophysicsstructural biologyvitamin uptake

Identifiers

PMID33350937
PMCPMC7755397
OpenAlexW3114959077

What OpenQuestion holds

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LicenceCC BY
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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.