Evidence map›Paper›PMID 18599740›Full record

ArticleScience (New York, N.Y.)2008

The crystal structure of a sodium galactose transporter reveals mechanistic insights into Na+/sugar symport.

Salem Faham, Akira Watanabe, Gabriel Mercado Besserer, Duilio Cascio, Alexandre Specht, Bruce A Hirayama, Ernest M Wright, Jeff Abramson

Abstract read
In one paragraph

Article in Science (New York, N.Y.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 290 papers.

0numbers the graph read from it
0cells of the map it votes in
290citing 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

290 citing papers in PubMed.

  1. Review
  2. Article
  3. Revisiting vSGLT: Non-Radioactive Characterization of the Vibrio NaInternational journal of molecular sciences · 2026
    Article
  4. Review
  5. Article
  6. Review
  7. Gliflozins in hypertension: basic mechanisms and clinical insights.American journal of physiology. Renal physiology · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Molecular mechanisms of NaBiophysical journal · 2024
    Article
  15. Conformational free-energy landscapes of a NaProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Identification ofInternational journal of molecular sciences · 2023
    Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Salem FahamDepartment of Physiology, David Geffen School of Medicine, University of California, Los Angeles, CA 90095-1751, USA.
Akira Watanabe
Gabriel Mercado Besserer
Duilio Cascio
Alexandre Specht
Bruce A Hirayama
Ernest M Wright
Jeff Abramson

Funding

Structures of sodium glucose transporters by cryo electron microscopyR01GM078844 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI ABRAMSON, JEFFREY S · 2006 to 2018
$5.3M
MOLECULAR MECHANISMS OF INTESTINAL TRANSPORTR01DK019567 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WRIGHT, ERNEST M · 1986 to 2013
$4.3M
MOLECULAR ARCHITECTURE OF THE NA/GLUCOSE COTRANSPORTERR01DK044602 · NIDDK · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WRIGHT, ERNEST M · 1992 to 2005
$1.5M
NIDDK NIH HHS DK19567NIDDK NIH HHS DK44602NIDDK NIH HHS R01 DK019567NIDDK NIH HHS R01 DK044602NIGMS NIH HHS GM07844NIGMS NIH HHS R01 GM078844
6 · The paper itself

Abstract

Membrane transporters that use energy stored in sodium gradients to drive nutrients into cells constitute a major class of proteins. We report the crystal structure of a member of the solute sodium symporters (SSS), the Vibrio parahaemolyticus sodium/galactose symporter (vSGLT). The approximately 3.0 angstrom structure contains 14 transmembrane (TM) helices in an inward-facing conformation with a core structure of inverted repeats of 5 TM helices (TM2 to TM6 and TM7 to TM11). Galactose is bound in the center of the core, occluded from the outside solutions by hydrophobic residues. Surprisingly, the architecture of the core is similar to that of the leucine transporter (LeuT) from a different gene family. Modeling the outward-facing conformation based on the LeuT structure, in conjunction with biophysical data, provides insight into structural rearrangements for active transport.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesBiological TransportCrystallography, X-RayDimerizationGalactoseHydrogen BondingHydrophobic and Hydrophilic InteractionsLipid BilayersModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondarySodiumSodium-Glucose Transport ProteinsBacterial ProteinsGalactoseLipid BilayersSodiumsodium glucose symporter, Vibrio parahaemolyticusSodium-Glucose Transport Proteins

Identifiers

PMID18599740
PMCPMC3654663

What OpenQuestion holds

Textmetadata
LicenceTDM
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.