Evidence map›Paper›PMID 19395376›Full record

ArticleThe Journal of biological chemistry2009

Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer.

Mathias Grote, Yevhen Polyhach, Gunnar Jeschke, Heinz-Jürgen Steinhoff, Erwin Schneider, Enrica Bordignon

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 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

35 citing papers in PubMed, 71 citations in OpenAlex.

  1. Article
  2. The Evolution of ABC Importers.Journal of molecular biology · 2025
    Review
  3. Article
  4. Article
  5. Orientation and dynamics of CuPhysical chemistry chemical physics : PCCP · 2020
    Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Structural diversity of ABC transporters.The Journal of general physiology · 2014
    Review
  15. Article
  16. Article
  17. Article
  18. Molecular mechanism of the Escherichia coli maltose transporter.Current opinion in structural biology · 2013
    Review
  19. Article
  20. Conformational plasticity of the type I maltose ABC importer.Proceedings of the National Academy of Sciences of the United States of America · 2013
    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

6 authors at 3 institutions in 2 countries.

Mathias GroteInstitut für Biologie/Bakterienphysiologie, Humboldt Universität zu Berlin, Chausseestrasse 117, D-10115 Berlin, Germany.
Yevhen Polyhach
Gunnar Jeschke
Heinz-Jürgen Steinhoff
Erwin Schneider
Enrica Bordignon
ETH Zurich · CHHumboldt-Universität zu Berlin · DEOsnabrück University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ABC transporters are ubiquitous membrane proteins that translocate solutes across biological membranes at the expense of ATP. In prokaryotic ABC importers, the extracytoplasmic anchoring of the substrate-binding protein (receptor) is emerging as a key determinant for the structural rearrangements in the cytoplasmically exposed ATP-binding cassette domains and in the transmembrane gates during the nucleotide cycle. Here the molecular mechanism of such signaling events was addressed by electron paramagnetic resonance spectroscopy of spin-labeled ATP-binding cassette maltose transporter variants (MalFGK2-E). A series of doubly spin-labeled mutants in the MalF-P2 domain involving positions 92, 205, 239, 252, and 273 and one triple mutant labeled at positions 205/252 in P2 and 83 in the Q-loop of MalK were assayed. The EPR data revealed that the substrate-binding protein MalE is bound to the transporter throughout the transport cycle. Concomitantly with the three conformations of the ATP-binding cassette MalK2, three functionally relevant conformations are found also in the periplasmic MalF-P2 loop, strictly dependent on cytoplasmic nucleotide binding and periplasmic docking of liganded MalE to MalFG. The reciprocal communication across the membrane unveiled here gives first insights into the stimulatory effect of MalE on the ATPase activity, and it is suggested to be an important mechanistic feature of receptor-coupled ABC transporters.

Indexed as

Adenosine TriphosphateATP-Binding Cassette TransportersCell MembraneDimerizationElectron Spin Resonance SpectroscopyEscherichia coliEscherichia coli ProteinsMaltoseModels, MolecularMonosaccharide Transport ProteinsMutagenesis, Site-DirectedPeriplasmProtein ConformationSignal TransductionAdenosine TriphosphateATP-Binding Cassette TransportersEscherichia coli ProteinsMalF protein, E coliMalG protein, E coliMalK protein, E coliMaltosemaltose transport system, E coliMonosaccharide Transport Proteins

Identifiers

PMID19395376
PMCPMC2719391
OpenAlexW2052146488

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.