Evidence map›Paper›PMID 19419962›Full record

ArticleThe Journal of biological chemistry2009

Substrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter.

Christian A Bippes, Antra Zeltina, Fabio Casagrande, Merce Ratera, Manuel Palacin, Daniel J Muller, Dimitrios Fotiadis

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
  2. Article
  3. Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Substrate-induced changes in the structural properties of LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  9. Review
  10. Article
  11. Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  12. Article
  13. Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  14. Article
  15. 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

7 authors at 5 institutions in 4 countries.

Christian A BippesBiotechnology Center, Technische Universität Dresden, D-01307 Dresden, Germany.
Antra Zeltina
Fabio Casagrande
Merce Ratera
Manuel Palacin
Daniel J Muller
Dimitrios Fotiadis
TU Dresden · DEInstitute for Research in Biomedicine · ESUniversitat de Barcelona · ESUniversity of Bern · CHUniversity of California, San Diego · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We used single molecule dynamic force spectroscopy to unfold individual serine/threonine antiporters SteT from Bacillus subtilis. The unfolding force patterns revealed interactions and energy barriers that stabilized structural segments of SteT. Substrate binding did not establish strong localized interactions but appeared to be facilitated by the formation of weak interactions with several structural segments. Upon substrate binding, all energy barriers of the antiporter changed thereby describing the transition from brittle mechanical properties of SteT in the unbound state to structurally flexible conformations in the substrate-bound state. The lifetime of the unbound state was much shorter than that of the substrate-bound state. This leads to the conclusion that the unbound state of SteT shows a reduced conformational flexibility to facilitate specific substrate binding and a reduced kinetic stability to enable rapid switching to the bound state. In contrast, the bound state of SteT showed an increased conformational flexibility and kinetic stability such as required to enable transport of substrate across the cell membrane. This result supports the working model of antiporters in which alternate substrate access from one to the other membrane surface occurs in the substrate-bound state.

Indexed as

Ion TransportAmino AcidsAntiportersBacillus subtilisBacterial ProteinsBinding SitesBiological TransportBiophysicsCloning, MolecularKineticsMolecular ConformationSubstrate SpecificityThermodynamicsAmino AcidsAntiportersBacterial Proteins

Identifiers

PMID19419962
PMCPMC2707244
OpenAlexW2024812079

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.