Evidence map›Paper›PMID 15339805›Full record

ArticleBiophysical journal2004

Structure and transport mechanism of the bacterial oxalate transporter OxlT.

Teruhisa Hirai, Sriram Subramaniam

Open access · bronzeAbstract readComparative StudyEvaluation StudyValidation Study
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
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

21 citing papers in PubMed, 61 citations in OpenAlex.

  1. Adaptively evolvedApplied and environmental microbiology · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. Applications of sequence coevolution in membrane protein biochemistry.Biochimica et biophysica acta. Biomembranes · 2018
    Review
  6. Diversity and ecology of oxalotrophic bacteria.World journal of microbiology & biotechnology · 2016
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural perspectives on secondary active transporters.Trends in pharmacological sciences · 2010
    Review
  15. Article
  16. Article
  17. Vitamin C transporters.Journal of physiology and biochemistry · 2008
    Review
  18. Review
  19. Article
  20. Experimental tests of a homology model for OxlT, the oxalate transporter of Oxalobacter formigenes.Proceedings of the National Academy of Sciences of the United States of America · 2005
    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

2 authors at 1 institution in 1 country.

Teruhisa HiraiLaboratory of Cell Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Sriram Subramaniam
National Institutes of Health · US

Funding

Imaging cellular assemblies with three-dimensional electron microscopyZIABC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 2009 to 2019
$8.0M
Imaging cellular assemblies with three-dimensional EMZ01BC010278 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI SUBRAMANIAM, SRIRAM · 1999 to 2008
$1.1M
6 · The paper itself

Abstract

Membrane proteins that belong to the major facilitator superfamily (MFS) are found in organisms across the evolutionary spectrum and mediate the transport of a variety of substrates ranging from small metabolites to neurotransmitters. The oxalate transporter (OxlT) is a representative MFS protein, and exchanges formate for oxalate across the cytoplasmic membrane of the organism Oxalobacter formigenes. Here, we present a structural model for the protein conformational changes that occur during oxalate transport by combining a three-dimensional map of the oxalate-bound, "closed" state of OxlT at 6.5 A determined by cryo-electron microscopy with a model of the "open" state of OxlT based on the atomic structures of the related transporters, glycerol-3-phosphate transporter (GlpT) and lactose permease (LacY). We demonstrate that the principal structural change associated with substrate transport is a concerted rocking movement of the two structurally similar halves of the protein relative to each other. Our structural model places two positively charged residues, Arg-272 and Lys-355 in the central cavity, suggesting that electrostatic interactions between these residues and the oxalate anion is a key step in generating the conformational change between the open and closed states of the transporter.

Indexed as

Models, ChemicalModels, MolecularAmino Acid SequenceBacterial ProteinsBiological Transport, ActiveComputer SimulationMembrane Transport ProteinsMolecular Sequence DataOxalatesProtein ConformationSequence AlignmentSequence Analysis, ProteinSequence Homology, Amino AcidStructure-Activity RelationshipBacterial ProteinsGlpT protein, E colilactose permeaseMembrane Transport ProteinsOxalatesOxlT protein, bacteria

Identifiers

PMID15339805
PMCPMC1304825
OpenAlexW2000283182

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.