Evidence map›Paper›PMID 35927235›Full record

ArticleNature communications2022

Structural and mechanistic analysis of a tripartite ATP-independent periplasmic TRAP transporter.

Martin F Peter, Jan A Ruland, Peer Depping, Niels Schneberger, Emmanuele Severi, Jonas Moecking, Karl Gatterdam, Sarah Tindall, Alexandre Durand, Veronika Heinz and 7 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
4.3field-weighted citation impact, top 4% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Lipid Trafficking in Diverse Bacteria.Accounts of chemical research · 2025
    Review
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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

17 authors at 4 institutions in 3 countries.

Martin F PeterInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.ORCID 0000-0001-6549-8127
Jan A RulandInstitute for Physical und Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53127, Bonn, Germany.ORCID 0000-0003-2766-0407
Peer DeppingInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.ORCID 0000-0002-5694-2393
Niels SchnebergerInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Emmanuele SeveriDepartment of Biology (Area 10), University of York, York, YO10 5YW, UK.ORCID 0000-0001-9750-5539
Jonas MoeckingInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.ORCID 0000-0001-5914-1359
Karl GatterdamInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.
Sarah TindallDepartment of Biology (Area 10), University of York, York, YO10 5YW, UK.
Alexandre DurandInstitut de Génétique et de Biologie Molecule et Cellulaire, 1 Rue Laurent Fries, 67404, Illkirch Cedex, France.ORCID 0000-0002-9173-6886
Veronika HeinzInstitute of Biophysics and Biophysical Chemistry, University of Regensburg, Universitätsstr. 31, 93053, Regensburg, Germany.ORCID 0000-0003-4084-7460
Jan Peter SiebrasseInstitute for Physical und Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53127, Bonn, Germany.
Paul-Albert KoenigCore Facility Nanobodies, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.ORCID 0000-0001-5995-2557
Matthias GeyerInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany.ORCID 0000-0002-7718-5002
Christine ZieglerInstitute of Biophysics and Biophysical Chemistry, University of Regensburg, Universitätsstr. 31, 93053, Regensburg, Germany.ORCID 0000-0003-3439-7213
Ulrich KubitscheckInstitute for Physical und Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53127, Bonn, Germany.ORCID 0000-0003-3750-5355
Gavin H ThomasDepartment of Biology (Area 10), University of York, York, YO10 5YW, UK.ORCID 0000-0002-9763-1313
Gregor HageluekenInstitute of Structural Biology, University of Bonn, Venusberg-Campus 1, 53127, Bonn, Germany. hagelueken@uni-bonn.de.ORCID 0000-0001-8781-5664
University of Bonn · DEUniversity of York · GBUniversity of Regensburg · DEInstitut de génétique et de biologie moléculaire et cellulaire · FR

Funding

Biotechnology and Biological Sciences Research Council BB/F014759/1
6 · The paper itself

Abstract

Tripartite ATP-independent periplasmic (TRAP) transporters are found widely in bacteria and archaea and consist of three structural domains, a soluble substrate-binding protein (P-domain), and two transmembrane domains (Q- and M-domains). HiSiaPQM and its homologs are TRAP transporters for sialic acid and are essential for host colonization by pathogenic bacteria. Here, we reconstitute HiSiaQM into lipid nanodiscs and use cryo-EM to reveal the structure of a TRAP transporter. It is composed of 16 transmembrane helices that are unexpectedly structurally related to multimeric elevator-type transporters. The idiosyncratic Q-domain of TRAP transporters enables the formation of a monomeric elevator architecture. A model of the tripartite PQM complex is experimentally validated and reveals the coupling of the substrate-binding protein to the transporter domains. We use single-molecule total internal reflection fluorescence (TIRF) microscopy in solid-supported lipid bilayers and surface plasmon resonance to study the formation of the tripartite complex and to investigate the impact of interface mutants. Furthermore, we characterize high-affinity single variable domains on heavy chain (VHH) antibodies that bind to the periplasmic side of HiSiaQM and inhibit sialic acid uptake, providing insight into how TRAP transporter function might be inhibited in vivo.

Indexed as

Bacterial ProteinsN-Acetylneuraminic AcidAdenosine TriphosphateArchaeaBacteriaCarrier ProteinsMembrane Transport ProteinsAdenosine TriphosphateBacterial ProteinsCarrier ProteinsMembrane Transport ProteinsN-Acetylneuraminic Acid

Identifiers

PMID35927235
PMCPMC9352664
OpenAlexW4289841189

What OpenQuestion holds

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LicenceCC BY
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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.