Evidence map›Paper›PMID 35767641›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Structural basis for heme detoxification by an ATP-binding cassette-type efflux pump in gram-positive pathogenic bacteria.

Hiro Nakamura, Tamao Hisano, Md Mahfuzur Rahman, Takehiko Tosha, Mikako Shirouzu, Yoshitsugu Shiro

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. 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
4.9field-weighted citation impact, top 4% 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, 27 citations in OpenAlex.

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  12. Review
  13. Maintenance of heme homeostasis inJournal of bacteriology · 2023
    Article
  14. Review
  15. Activator-induced conformational changes regulate division-associated peptidoglycan amidases.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

6 authors at 3 institutions in 1 country.

Hiro NakamuraLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama 230-0045, Japan.ORCID 0000-0001-6914-3411
Tamao HisanoLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama 230-0045, Japan.ORCID 0000-0002-5832-8442
Md Mahfuzur RahmanBiometal Science Laboratory, RIKEN SPring-8 Center, Hyogo 679-5148, Japan.ORCID 0000-0003-1816-2422
Takehiko ToshaBiometal Science Laboratory, RIKEN SPring-8 Center, Hyogo 679-5148, Japan.ORCID 0000-0002-8971-0759
Mikako ShirouzuLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, Yokohama 230-0045, Japan.ORCID 0000-0002-7997-2149
Yoshitsugu ShiroBiometal Science Laboratory, RIKEN SPring-8 Center, Hyogo 679-5148, Japan.ORCID 0000-0003-0695-8327
SPring-8 · JPUniversity of Hyogo · JPRIKEN Center for Biosystems Dynamics Research · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Bacterial pathogens acquire heme from the host hemoglobin as an iron nutrient for their virulence and proliferation in blood. Concurrently, they encounter cytotoxic-free heme that escapes the heme-acquisition process. To overcome this toxicity, many gram-positive bacteria employ an ATP-binding cassette heme-dedicated efflux pump, HrtBA in the cytoplasmic membranes. Although genetic analyses have suggested that HrtBA expels heme from the bacterial membranes, the molecular mechanism of heme efflux remains elusive due to the lack of protein studies. Here, we show the biochemical properties and crystal structures of

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCorynebacterium diphtheriaeHemeMembrane Transport ProteinsAdenosine TriphosphateProtein ConformationProtein MultimerizationAdenosine TriphosphatasesAdenosine TriphosphateBacterial ProteinsHemeMembrane Transport ProteinsABC transporterhemeheme toxicitymembranepathogenic bacteria

Identifiers

PMID35767641
PMCPMC9271180
OpenAlexW4283704767

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.