Evidence map›Paper›PMID 25686089›Full record

ArticleNature structural & molecular biology2015

Crystal structure of a phosphorylation-coupled vitamin C transporter.

Ping Luo, Xinzhe Yu, Weiguang Wang, Shilong Fan, Xiaochun Li, Jiawei Wang

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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. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020
    Review
  7. Elevator-type mechanisms of membrane transport.Biochemical Society transactions · 2020
    Review
  8. Article
  9. Article
  10. Structure of an EIIC sugar transporter trapped in an inward-facing conformation.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

6 authors.

Ping Luo1] State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China. [2] Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Xinzhe Yu1] Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China. [2] Ministry of Education Key Laboratory of Protein Science, School of Life Sciences, Tsinghua University, Beijing, China.
Weiguang Wang1] State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China. [2] Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Shilong FanCenter for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.
Xiaochun LiLaboratory of Cell Biology, Rockefeller University, New York, New York, USA.
Jiawei Wang1] State Key Laboratory of Biomembrane and Membrane Biotechnology, School of Life Sciences, Tsinghua University, Beijing, China. [2] Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacteria use vitamin C (L-ascorbic acid) as a carbon source under anaerobic conditions. The phosphoenolpyruvate-dependent phosphotransferase system (PTS), comprising a transporter (UlaA), a IIB-like enzyme (UlaB) and a IIA-like enzyme (UlaC), is required for the anaerobic uptake of vitamin C and its phosphorylation to L-ascorbate 6-phosphate. Here, we present the crystal structures of vitamin C-bound UlaA from Escherichia coli in two conformations at 1.65-Å and 2.35-Å resolution. UlaA forms a homodimer and exhibits a new fold. Each UlaA protomer consists of 11 transmembrane segments arranged into a 'V-motif' domain and a 'core' domain. The V motifs form the interface between the two protomers, and the core-domain residues coordinate vitamin C. The alternating access of the substrate from the opposite side of the cell membrane may be achieved through rigid-body rotation of the core relative to the V motif.

Indexed as

Ascorbic AcidBinding SitesBiological TransportCrystallography, X-RayEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularPhosphorylationProtein Structure, TertiaryAscorbic AcidEscherichia coli ProteinsMembrane Transport ProteinsSgaT protein, E coli

Identifiers

PMID25686089

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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.