Evidence map›Paper›PMID 36849793›Full record

ArticleNature communications2023

Structure and mechanism of a tripartite ATP-independent periplasmic TRAP transporter.

James S Davies, Michael J Currie, Rachel A North, Mariafrancesca Scalise, Joshua D Wright, Jack M Copping, Daniela M Remus, Ashutosh Gulati, Dustin R Morado, Sam A Jamieson and 10 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
10.6field-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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  4. ChronicInternational journal of molecular sciences · 2025
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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

20 authors at 10 institutions in 5 countries.

James S Davies *Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID 0000-0003-4029-1650
Michael J Currie *Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.ORCID 0000-0003-1509-7581
Rachel A North *Biomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand. rachel.north@dbb.su.se.ORCID 0000-0001-5011-1567
Mariafrancesca ScaliseDepartment DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via P. Bucci 4C, 87036, Arcavacata di Rende, Italy.ORCID 0000-0003-3860-6844
Joshua D WrightBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Jack M CoppingBiomolecular Interaction Centre, Digital Life Institute, Maurice Wilkins Centre for Molecular Biodiscovery, and School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand.
Daniela M RemusBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Ashutosh GulatiDepartment of Biochemistry and Biophysics, Stockholm University, 10691, Stockholm, Sweden.ORCID 0000-0003-0960-994X
Dustin R MoradoScience for Life Laboratory, Department of Biochemistry and Biophysics, Stockholm University, 17165, Solna, Sweden.
Sam A JamiesonBiochemistry Department, School of Biomedical Sciences, University of Otago, Dunedin, 9054, New Zealand.ORCID 0000-0003-0120-4737
Michael C Newton-VestyBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Gayan S AbeysekeraBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand.
Subramanian RamaswamyBiological Sciences and Biomedical Engineering, Bindley Bioscience Center, Purdue University, 1203 W State St, West Lafayette, IN 47906, USA.ORCID 0000-0002-6709-190X
Rosmarie FriemannCentre for Antibiotic Resistance Research (CARe) at University of Gothenburg, Box 440, S-40530, Gothenburg, Sweden.
Soichi WakatsukiBiological Sciences Division, SLAC National Accelerator Laboratory, Menlo Park, CA, 94025, USA.ORCID 0000-0001-5896-7968
Jane R AllisonBiomolecular Interaction Centre, Digital Life Institute, Maurice Wilkins Centre for Molecular Biodiscovery, and School of Biological Sciences, University of Auckland, Auckland, 1010, New Zealand.ORCID 0000-0002-5699-1726
Cesare IndiveriDepartment DiBEST (Biologia, Ecologia, Scienze della Terra) Unit of Biochemistry and Molecular Biotechnology, University of Calabria, Via P. Bucci 4C, 87036, Arcavacata di Rende, Italy.
David DrewDepartment of Biochemistry and Biophysics, Stockholm University, 10691, Stockholm, Sweden.
Peter D MaceBiochemistry Department, School of Biomedical Sciences, University of Otago, Dunedin, 9054, New Zealand.ORCID 0000-0003-2175-9537
Renwick C J DobsonBiomolecular Interaction Centre, Maurice Wilkins Centre for Biodiscovery, MacDiarmid Institute for Advanced Materials and Nanotechnology and School of Biological Sciences, University of Canterbury, PO Box 4800, Christchurch, 8140, New Zealand. renwick.dobson@canterbury.ac.nz.ORCID 0000-0002-5506-4939
Stockholm University · SEUniversity of Canterbury · NZUniversity of Auckland · NZUniversity of Otago · NZBiotechnology Institute · USInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · ITPurdue University West Lafayette · USSLAC National Accelerator Laboratory · USUniversity of Calabria · ITUniversity of Gothenburg · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria and archaea, tripartite ATP-independent periplasmic (TRAP) transporters uptake essential nutrients. TRAP transporters receive their substrates via a secreted soluble substrate-binding protein. How a sodium ion-driven secondary active transporter is strictly coupled to a substrate-binding protein is poorly understood. Here we report the cryo-EM structure of the sialic acid TRAP transporter SiaQM from Photobacterium profundum at 2.97 Å resolution. SiaM comprises a "transport" domain and a "scaffold" domain, with the transport domain consisting of helical hairpins as seen in the sodium ion-coupled elevator transporter VcINDY. The SiaQ protein forms intimate contacts with SiaM to extend the size of the scaffold domain, suggesting that TRAP transporters may operate as monomers, rather than the typically observed oligomers for elevator-type transporters. We identify the Na

Indexed as

Membrane Transport ProteinsN-Acetylneuraminic AcidAdenosine TriphosphateArchaeaBiological TransportAdenosine TriphosphateMembrane Transport ProteinsN-Acetylneuraminic Acid

Identifiers

PMID36849793
PMCPMC9971032
OpenAlexW4322490033

What OpenQuestion holds

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LicenceCC BY
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.