Evidence map›Paper›PMID 25088546›Full record

ArticleNature communications2014

Proton-coupled sugar transport in the prototypical major facilitator superfamily protein XylE.

Goragot Wisedchaisri, Min-Sun Park, Matthew G Iadanza, Hongjin Zheng, Tamir Gonen

Abstract read
In one paragraph

Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing 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

88 citing papers in PubMed.

  1. Article
  2. EngineeringSynthetic and systems biotechnology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026
    Article
  8. Article
  9. Article
  10. Maltose and Maltotriose Transporters in Brewer'sInternational journal of molecular sciences · 2025
    Review
  11. Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

28 more citing papers are in PubMed but not listed here.

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.

Goragot Wisedchaisri1] Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20147, USA [2].
Min-Sun Park1] Janelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20147, USA [2].
Matthew G IadanzaJanelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20147, USA.
Hongjin ZhengJanelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20147, USA.
Tamir GonenJanelia Research Campus, Howard Hughes Medical Institute, 19700 Helix Drive, Ashburn, Virginia 20147, USA.

Funding

X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Howard Hughes Medical InstituteNIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393
6 · The paper itself

Abstract

The major facilitator superfamily (MFS) is the largest collection of structurally related membrane proteins that transport a wide array of substrates. The proton-coupled sugar transporter XylE is the first member of the MFS that has been structurally characterized in multiple transporting conformations, including both the outward and inward-facing states. Here we report the crystal structure of XylE in a new inward-facing open conformation, allowing us to visualize the rocker-switch movement of the N-domain against the C-domain during the transport cycle. Using molecular dynamics simulation, and functional transport assays, we describe the movement of XylE that facilitates sugar translocation across a lipid membrane and identify the likely candidate proton-coupling residues as the conserved Asp27 and Arg133. This study addresses the structural basis for proton-coupled substrate transport and release mechanism for the sugar porter family of proteins.

Indexed as

ProtonsArginineAspartic AcidBiological TransportEscherichia coliEscherichia coli ProteinsGene ExpressionHydrogen BondingLipid BilayersMolecular Dynamics SimulationPhosphatidylcholinesProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsSymportersThermodynamics1-palmitoyl-2-oleoylphosphatidylcholineArginineAspartic AcidEscherichia coli ProteinsLipid BilayersPhosphatidylcholinesProtonsRecombinant ProteinsSymportersxylE protein, E coliXylose

Identifiers

PMID25088546
PMCPMC4137407

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.