Evidence map›Paper›PMID 16952940›Full record

ArticleJournal of bacteriology2006

Tungsten transport protein A (WtpA) in Pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters.

Loes E Bevers, Peter-Leon Hagedoorn, Gerard C Krijger, Wilfred R Hagen

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-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

30 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Tungsten enzymes play a role in detoxifying food and antimicrobial aldehydes in the human gut microbiome.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Characterization of a Metal-ResistantFrontiers in microbiology · 2020
    Article
  9. Determination of Ligand Profiles forInternational journal of molecular sciences · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Acquisition and role of molybdate in Pseudomonas aeruginosa.Applied and environmental microbiology · 2014
    Article
  17. Article
  18. Binding of ReO4(-) with an engineered MoO4(2-)-binding protein: towards a new approach in radiopharmaceutical applications.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  19. Article
  20. 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

4 authors at 1 institution in 1 country.

Loes E BeversDepartment of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands.
Peter-Leon Hagedoorn
Gerard C Krijger
Wilfred R Hagen
Delft University of Technology · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A novel tungstate and molybdate binding protein has been discovered from the hyperthermophilic archaeon Pyrococcus furiosus. This tungstate transport protein A (WtpA) is part of a new ABC transporter system selective for tungstate and molybdate. WtpA has very low sequence similarity with the earlier-characterized transport proteins ModA for molybdate and TupA for tungstate. Its structural gene is present in the genome of numerous archaea and some bacteria. The identification of this new tungstate and molybdate binding protein clarifies the mechanism of tungstate and molybdate transport in organisms that lack the known uptake systems associated with the ModA and TupA proteins, like many archaea. The periplasmic protein of this ABC transporter, WtpA (PF0080), was cloned and expressed in Escherichia coli. Using isothermal titration calorimetry, WtpA was observed to bind tungstate (dissociation constant [K(D)] of 17 +/- 7 pM) and molybdate (K(D) of 11 +/- 5 nM) with a stoichiometry of 1.0 mol oxoanion per mole of protein. These low K(D) values indicate that WtpA has a higher affinity for tungstate than do ModA and TupA and an affinity for molybdate similar to that of ModA. A displacement titration of molybdate-saturated WtpA with tungstate showed that the tungstate effectively replaced the molybdate in the binding site of the protein.

Indexed as

Amino Acid SequenceArchaeal ProteinsATP-Binding Cassette TransportersBacterial ProteinsCloning, MolecularEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsMolecular Sequence DataMolybdenumPeriplasmic Binding ProteinsPeriplasmic ProteinsPhylogenyProtein BindingPyrococcus furiosusSequence Homology, Amino AcidArchaeal ProteinsATP-Binding Cassette TransportersBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsModA protein, E colimolybdateMolybdenumPeriplasmic Binding ProteinsPeriplasmic ProteinstungstateTungsten CompoundsTupA protein, Eubacterium acidaminophilum

Identifiers

PMID16952940
PMCPMC1595483
OpenAlexW1990989901

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.