Evidence map›Paper›PMID 18395745›Full record

ArticleJournal of molecular biology2008

Salt-bridge dynamics control substrate-induced conformational change in the membrane transporter GlpT.

Christopher J Law, Jonas Almqvist, Adam Bernstein, Regina M Goetz, Yafei Huang, Celine Soudant, Aatto Laaksonen, Sven Hovmöller, Da-Neng Wang

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

32 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
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  4. GLUT5: structure, functions, diseases and potential applications.Acta biochimica et biophysica Sinica · 2023
    Review
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  14. Cotranslational folding of membrane proteins probed by arrest-peptide-mediated force measurements.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  15. Review
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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

9 authors at 3 institutions in 2 countries.

Christopher J LawThe Helen L. and Martin S. Kimmel Center for Biology and Medicine, Skirball Institute of Biomolecular Medicine, Department of Cell Biology, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA.
Jonas Almqvist
Adam Bernstein
Regina M Goetz
Yafei Huang
Celine Soudant
Aatto Laaksonen
Sven Hovmöller
Da-Neng Wang
New York University · USStockholm University · SESwedish University of Agricultural Sciences · SE

Funding

STRUCTURAL STUDIES OF SUGAR TRANSPORTERSR01DK053973 · NIDDK · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 1998 to 2014
$3.6M
Structural and Mechanistic Characterization of Neurotransmitter Reuptake InhibitiR01MH083840 · NIMH · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WANG, DANENG · 2008 to 2012
$2.2M
NIDDK NIH HHS DK-053973NIDDK NIH HHS R01 DK053973
6 · The paper itself

Abstract

Active transport of substrates across cytoplasmic membranes is of great physiological, medical and pharmaceutical importance. The glycerol-3-phosphate (G3P) transporter (GlpT) of the E. coli inner membrane is a secondary active antiporter from the ubiquitous major facilitator superfamily that couples the import of G3P to the efflux of inorganic phosphate (P(i)) down its concentration gradient. Integrating information from a novel combination of structural, molecular dynamics simulations and biochemical studies, we identify the residues involved directly in binding of substrate to the inward-facing conformation of GlpT, thus defining the structural basis for the substrate-specificity of this transporter. The substrate binding mechanism involves protonation of a histidine residue at the binding site. Furthermore, our data suggest that the formation and breaking of inter- and intradomain salt bridges control the conformational change of the transporter that accompanies substrate translocation across the membrane. The mechanism we propose may be a paradigm for organophosphate:phosphate antiporters.

Indexed as

Amino AcidsBinding SitesComputer SimulationCrystallography, X-RayKineticsMembrane Transport ProteinsModels, MolecularMutationProtein Structure, TertiaryProtonsSodium ChlorideAmino AcidsGlpT protein, E coliMembrane Transport ProteinsProtonsSodium Chloride

Identifiers

PMID18395745
PMCPMC2426824
OpenAlexW2114090589

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.