Evidence map›Paper›PMID 23075985›Full record

ArticleNature2012

Crystal structure of a bacterial homologue of glucose transporters GLUT1-4.

Linfeng Sun, Xin Zeng, Chuangye Yan, Xiuyun Sun, Xinqi Gong, Yu Rao, Nieng Yan

Abstract read
PubMed Publisher
In one paragraph

Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 254 papers.

0numbers the graph read from it
0cells of the map it votes in
254citing 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

254 citing papers in PubMed.

  1. Review
  2. Article
  3. Structure and allostery in major facilitator superfamily symport mechanisms.Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Article
  5. Review
  6. Article
  7. A two-step mechanism for sugar translocation.Nature structural & molecular biology · 2026
    Article
  8. Article
  9. Comprehensive Insights into Sugar Transporters ofJournal of fungi (Basel, Switzerland) · 2026
    Article
  10. Article
  11. Structural basis of glucose-6-phosphate transport by human SLC37A2.Nature structural & molecular biology · 2026
    Article
  12. Allosteric effects of the coupling cation in melibiose transporter MelB.bioRxiv : the preprint server for biology · 2025
    Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Identification of New Key Players for Ferrous Iron Export in the Asymmetric Inner Gate of Human Ferroportin 1.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Article
  18. Article
  19. 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
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Linfeng SunState Key Laboratory of Bio-membrane and Membrane Biotechnology, Center for Structural Biology, Tsinghua University, Beijing 100084, China.
Xin Zeng
Chuangye Yan
Xiuyun Sun
Xinqi Gong
Yu Rao
Nieng Yan

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glucose transporters are essential for metabolism of glucose in cells of diverse organisms from microbes to humans, exemplified by the disease-related human proteins GLUT1, 2, 3 and 4. Despite rigorous efforts, the structural information for GLUT1-4 or their homologues remains largely unknown. Here we report three related crystal structures of XylE, an Escherichia coli homologue of GLUT1-4, in complex with d-xylose, d-glucose and 6-bromo-6-deoxy-D-glucose, at resolutions of 2.8, 2.9 and 2.6 Å, respectively. The structure consists of a typical major facilitator superfamily fold of 12 transmembrane segments and a unique intracellular four-helix domain. XylE was captured in an outward-facing, partly occluded conformation. Most of the important amino acids responsible for recognition of D-xylose or d-glucose are invariant in GLUT1-4, suggesting functional and mechanistic conservations. Structure-based modelling of GLUT1-4 allows mapping and interpretation of disease-related mutations. The structural and biochemical information reported here constitutes an important framework for mechanistic understanding of glucose transporters and sugar porters in general.

Indexed as

Biological TransportCrystallography, X-RayDeoxyglucoseEscherichia coliEscherichia coli ProteinsGlucoseGlucose Transporter Type 1Glucose Transport Proteins, FacilitativeHumansHydrogen BondingModels, MolecularProtein ConformationStructural Homology, ProteinStructure-Activity RelationshipSubstrate SpecificitySymporters6-bromo-6-deoxy-D-glucoseDeoxyglucoseEscherichia coli ProteinsGlucoseGlucose Transporter Type 1Glucose Transport Proteins, FacilitativeSLC2A1 protein, humanSymportersxylE protein, E coliXylose

Identifiers

PMID23075985

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.