Evidence map›Paper›PMID 15175304›Full record

ArticleJournal of bacteriology2004

Structural basis for iron binding and release by a novel class of periplasmic iron-binding proteins found in gram-negative pathogens.

Stephen R Shouldice, Robert J Skene, Douglas R Dougan, Gyorgy Snell, Duncan E McRee, Anthony B Schryvers, Leslie W Tari

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

19 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Structural and functional insights into iron acquisition from lactoferrin and transferrin in Gram-negative bacterial pathogens.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  3. Iron Reduction inInternational journal of molecular sciences · 2022
    Article
  4. Structural dynamics in the evolution of a bilobed protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  5. Article
  6. Article
  7. Frontiers in microbiology · 2018
    Article
  8. Article
  9. Beyond iron: non-classical biological functions of bacterial siderophores.Dalton transactions (Cambridge, England : 2003) · 2015
    Review
  10. Review
  11. Ferric ion (hydr)oxo clusters in the "Venus flytrap" cleft of FbpA: Mössbauer, calorimetric and mass spectrometric studies.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2012
    Article
  12. Article
  13. Expression, crystallization and preliminary X-ray analysis of a ferric binding protein from Thermus thermophilus HB8.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  14. Photolysis of iron-siderophore chelates promotes bacterial-algal mutualism.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Diversity in ABC transporters: type I, II and III importers.Critical reviews in biochemistry and molecular biology
    Review
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 1 institution in 1 country.

Stephen R ShouldiceDepartment of Microbiology and Infectious Diseases, University of Calgary, Calgary, AB, Canada.
Robert J Skene
Douglas R Dougan
Gyorgy Snell
Duncan E McRee
Anthony B Schryvers
Leslie W Tari
University of Calgary · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have determined the 1.35- and 1.45-A structures, respectively, of closed and open iron-loaded forms of Mannheimia haemolytica ferric ion-binding protein A. M. haemolytica is the causative agent in the economically important and fatal disease of cattle termed shipping fever. The periplasmic iron-binding protein of this gram-negative bacterium, which has homologous counterparts in many other pathogenic species, performs a key role in iron acquisition from mammalian host serum iron transport proteins and is essential for the survival of the pathogen within the host. The ferric (Fe(3+)) ion in the closed structure is bound by a novel asymmetric constellation of four ligands, including a synergistic carbonate anion. The open structure is ligated by three tyrosyl residues and a dynamically disordered solvent-exposed anion. Our results clearly implicate the synergistic anion as the primary mediator of global protein conformation and provide detailed insights into the molecular mechanisms of iron binding and release in the periplasm.

Indexed as

AnimalsBacterial Outer Membrane ProteinsBacterial ProteinsCattleCrystallizationFerric CompoundsIronIron-Binding ProteinsMannheimia haemolyticaModels, MolecularMolecular Sequence DataPeriplasmPeriplasmic Binding ProteinsProtein ConformationX-Ray DiffractionBacterial Outer Membrane ProteinsBacterial ProteinsFerric CompoundsIronIron-Binding ProteinsPeriplasmic Binding Proteins

Identifiers

PMID15175304
PMCPMC419930
OpenAlexW2026990924

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.