Evidence map›Paper›PMID 25848002›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Structural basis for substrate specificity of an amino acid ABC transporter.

Jie Yu, Jingpeng Ge, Johanna Heuveling, Erwin Schneider, Maojun Yang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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
–field-weighted citation impact
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.

  1. Article
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  5. Review
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  8. Adaptive laboratory evolution ofFood chemistry: X · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Allosteric regulation of nitrate transporter NRT via the signaling protein PII.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Bacteria with a mouth: Discovery and new insights into cell surface structure and macromolecule transport.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2022
    Article
  17. Article
  18. Secretome Analysis ofProteomes · 2021
    Article
  19. 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

5 authors.

Jie YuMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China and.
Jingpeng GeMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China and.
Johanna HeuvelingDivision of Microbial Physiology, Department of Biology, Humboldt University of Berlin, D-10099 Berlin, Germany.
Erwin SchneiderDivision of Microbial Physiology, Department of Biology, Humboldt University of Berlin, D-10099 Berlin, Germany erwin.schneider@rz.hu-berlin.de maojunyang@tsinghua.edu.cn.
Maojun YangMinistry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China and erwin.schneider@rz.hu-berlin.de maojunyang@tsinghua.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP-binding cassette (ABC) transporters are ubiquitous integral membrane proteins that translocate a variety of substrates, ranging from ions to macromolecules, either out of or into the cytosol (hence defined as importers or exporters, respectively). It has been demonstrated that ABC exporters and importers function through a common mechanism involving conformational switches between inward-facing and outward-facing states; however, the mechanism underlying their functions, particularly substrate recognition, remains elusive. Here we report the structures of an amino acid ABC importer Art(QN)2 from Thermoanaerobacter tengcongensis composed of homodimers each of the transmembrane domain ArtQ and the nucleotide-binding domain ArtN, either in its apo form or in complex with substrates (Arg, His) and/or ATPs. The structures reveal that the straddling of the TMDs around the twofold axis forms a substrate translocation pathway across the membrane. Interestingly, each TMD has a negatively charged pocket that together create a negatively charged internal tunnel allowing amino acids carrying positively charged groups to pass through. Our structural and functional studies provide a better understanding of how ABC transporters select and translocate their substrates.

Indexed as

Adenosine TriphosphateApoproteinsArginineATP-Binding Cassette TransportersBinding SitesLigandsModels, MolecularProtein SubunitsStructure-Activity RelationshipSubstrate SpecificityThermoanaerobacterAdenosine TriphosphateApoproteinsArginineATP-Binding Cassette TransportersLigandsProtein SubunitsABC transportersinward-facing statesubstrate selectivitytwo binding sitestype I importer

Identifiers

PMID25848002
PMCPMC4413293

What OpenQuestion holds

Textmetadata
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.