Evidence map›Paper›PMID 19144921›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Heme uptake across the outer membrane as revealed by crystal structures of the receptor-hemophore complex.

Stefanie Krieg, Frédéric Huché, Kay Diederichs, Nadia Izadi-Pruneyre, Anne Lecroisey, Cécile Wandersman, Philippe Delepelaire, Wolfram Welte

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

75 citing papers in PubMed, 165 citations in OpenAlex.

  1. Article
  2. Structural basis of iron piracy by human gutProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Article
  8. Review
  9. Chaperone-assisted cryo-EM structure ofbioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. First report of whole genome sequence of septicemic Pasteurella multocida serovar B:2 'Soron' strain isolated from swine.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  13. Review
  14. Article
  15. Pirates of the haemoglobin.Microbial cell (Graz, Austria) · 2022
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020
    Review

15 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 3 countries.

Stefanie KriegFachbereich Biologie, Universität Konstanz, 78457 Konstanz, Germany.
Frédéric Huché
Kay Diederichs
Nadia Izadi-Pruneyre
Anne Lecroisey
Cécile Wandersman
Philippe Delepelaire
Wolfram Welte
The University of Texas Southwestern Medical Center · USUniversity of Konstanz · DECentre National de la Recherche Scientifique · FRInstitut Pasteur · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Gram-negative bacteria use specific heme uptake systems, relying on outer membrane receptors and excreted heme-binding proteins (hemophores) to scavenge and actively transport heme. To unravel the unknown molecular details involved, we present 3 structures of the Serratia marcescens receptor HasR in complex with its hemophore HasA. The transfer of heme over a distance of 9 A from its high-affinity site in HasA into a site of lower affinity in HasR is coupled with the exergonic complex formation of the 2 proteins. Upon docking to the receptor, 1 of the 2 axial heme coordinations of the hemophore is initially broken, but the position and orientation of the heme is preserved. Subsequently, steric displacement of heme by a receptor residue ruptures the other axial coordination, leading to heme transfer into the receptor.

Indexed as

ApoproteinsBacterial ProteinsBiological TransportCalorimetryCarrier ProteinsCell MembraneCrystallography, X-RayHemeHeme-Binding ProteinsHemeproteinsLigandsMembrane ProteinsModels, MolecularProtein Structure, SecondaryReceptors, Cell SurfaceSerratia marcescensApoproteinsBacterial ProteinsCarrier ProteinsHasA protein, Serratia marcescensHemeHeme-Binding ProteinsHemeproteinsLigandsMembrane ProteinsReceptors, Cell Surface

Identifiers

PMID19144921
PMCPMC2633585
OpenAlexW2067218778

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.