Evidence map›Paper›PMID 25787075›Full record

ArticleThe Journal of biological chemistry2015

Transcriptional Regulation, Metal Binding Properties and Structure of Pden1597, an Unusual Zinc Transport Protein from Paracoccus denitrificans.

Melody Handali, Durga P Neupane, Hridindu Roychowdhury, Erik T Yukl

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

16 citing papers in PubMed, 21 citations in OpenAlex.

  1. Two zinc ABC transporters contribute toFrontiers in plant science · 2025
    Article
  2. Zinc acquisition and its contribution toFrontiers in cellular and infection microbiology · 2023
    Article
  3. Structure and Function of the Zinc Binding Protein ZrgA fromInternational journal of molecular sciences · 2022
    Article
  4. Conformational flexibility in the zinc solute-binding protein ZnuA.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  5. Article
  6. Review
  7. Conformation of the Solute-Binding Protein AdcAII Influences Zinc Uptake inFrontiers in cellular and infection microbiology · 2021
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Frontiers in microbiology · 2018
    Article
  13. Article
  14. Article
  15. Zinc-Dependent Transcriptional Regulation inFrontiers in microbiology · 2017
    Article
  16. 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.

Melody HandaliFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Durga P NeupaneFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Hridindu RoychowdhuryFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003.
Erik T YuklFrom the Department of Chemistry and Biochemistry, New Mexico State University, Las Cruces, New Mexico 88003 etyukl@nmsu.edu.
New Mexico State University · US

Funding

Characterization of Accessory Factors in Bacterial Transition Metal ImportSC2GM111170 · NIGMS · NEW MEXICO STATE UNIVERSITY LAS CRUCES · PI YUKL, ERIK T · 2014 to 2016
$411k
Howard Hughes Medical InstituteNIGMS NIH HHS SC2 GM111170NIGMS NIH HHS SC2 GM111170-01
6 · The paper itself

Abstract

ATP-binding cassette (ABC) transporters of the cluster 9 family are ubiquitous among bacteria and essential for acquiring Zn(2+) and Mn(2+) from the environment or, in the case of pathogens, from the host. These rely on a substrate-binding protein (SBP) to coordinate the relevant metal with high affinity and specificity and subsequently release it to a membrane permease for translocation into the cytoplasm. Although a number of cluster 9 SBP structures have been determined, the structural attributes conferring Zn(2+) or Mn(2+) specificity remain ambiguous. Here we describe the gene expression profile, in vitro metal binding properties, and crystal structure of a new cluster 9 SBP from Paracoccus denitrificans we have called AztC. Although all of our results strongly indicate Zn(2+) over Mn(2+) specificity, the Zn(2+) ion is coordinated by a conserved Asp residue only observed to date as a metal ligand in Mn(2+)-specific SBPs. The unusual sequence properties of this protein are shared among close homologues, including members from the human pathogens Klebsiella pneumonia and Enterobacter aerogenes, and would seem to suggest a subclass of Zn(2+)-specific transporters among the cluster 9 family. In any case, the unusual coordination environment of AztC expands the already considerable range of those available to Zn(2+)-specific SBPs and highlights the presence of a His-rich loop as the most reliable indicator of Zn(2+) specificity.

Indexed as

Amino Acid SequenceBacterial ProteinsBinding SitesCation Transport ProteinsCircular DichroismGene Expression ProfilingManganeseMetalsMolecular Sequence DataParacoccus denitrificansPhylogenyProtein BindingProtein Structure, TertiarySequence Homology, Amino AcidZincBacterial ProteinsCation Transport ProteinsManganeseMetalsZincABC TransporterManganeseMetal HomeostasisMetalloproteinTranscription RegulationZinc

Identifiers

PMID25787075
PMCPMC4424328
OpenAlexW1999123993

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.