Evidence map›Paper›PMID 21611125›Full record

ArticlePloS one2011

Insight into the interaction of metal ions with TroA from Streptococcus suis.

Beiwen Zheng, Qiangmin Zhang, Jia Gao, Huiming Han, Ming Li, Jingren Zhang, Jianxun Qi, Jinghua Yan, George F Gao

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.4field-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

27 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  4. Review
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  8. Review
  9. Article
  10. Structure and Metal Binding Properties ofJournal of bacteriology · 2019
    Article
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  18. Host-imposed manganese starvation of invading pathogens: two routes to the same destination.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015
    Review
  19. Manganese uptake and streptococcal virulence.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015
    Review
  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

9 authors at 4 institutions in 1 country.

Beiwen ZhengCAS Key Laboratory of Pathogenic Microbiology and Immunology, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China.
Qiangmin Zhang
Jia Gao
Huiming Han
Ming Li
Jingren Zhang
Jianxun Qi
Jinghua Yan
George F Gao
Chinese Academy of Sciences · CNUniversity of Chinese Academy of Sciences · CNInstitute of Microbiology · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundThe scavenging ability of sufficient divalent metal ions is pivotal for pathogenic bacteria to survive in the host. ATP-binding cassette (ABC)-type metal transporters provide a considerable amount of different transition metals for bacterial growth. TroA is a substrate binding protein for uptake of multiple metal ions. However, the function and structure of the TroA homologue from the epidemic Streptococcus suis isolates (SsTroA) have not been characterized. METHODOLOGY/PRINCIPAL

findingsHere we determined the crystal structure of SsTroA from a highly pathogenic streptococcal toxic shock syndrome (STSS)-causing Streptococcus suis in complex with zinc. Inductively coupled plasma mass spectrometry (ICP-MS) analysis revealed that apo-SsTroA binds Zn(2+) and Mn(2+). Both metals bind to SsTroA with nanomolar affinity and stabilize the protein against thermal unfolding. Zn(2+) and Mn(2+) induce distinct conformational changes in SsTroA compared with the apo form as confirmed by both circular dichroism (CD) and nuclear magnetic resonance (NMR) spectra. NMR data also revealed that Zn(2+)/Mn(2+) bind to SsTroA in either the same site or an adjacent region. Finally, we found that the folding of the metal-bound protein is more compact than the corresponding apoprotein. CONCLUSIONS/SIGNIFICANCE: Our findings reveal a mechanism for uptake of metal ions in S. suis and this mechanism provides a reasonable explanation as to how SsTroA operates in metal transport.

Indexed as

Amino Acid SequenceAnilino NaphthalenesulfonatesBacterial ProteinsBinding SitesCalorimetryCircular DichroismCloning, MolecularComputational BiologyCrystallography, X-RayElectron Spin Resonance SpectroscopyFluorescenceIonsMagnetic Resonance SpectroscopyManganeseMetalsModels, Biological1-anilino-8-naphthalenesulfonateAnilino NaphthalenesulfonatesBacterial ProteinsIonsManganeseMetalsZinc

Identifiers

PMID21611125
PMCPMC3097204
OpenAlexW2080016346

What OpenQuestion holds

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LicenceCC BY
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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.