Evidence map›Paper›PMID 29129383›Full record

ArticleStructure (London, England : 1993)2017

The Structure of a Conserved Domain of TamB Reveals a Hydrophobic β Taco Fold.

Inokentijs Josts, Christopher James Stubenrauch, Grishma Vadlamani, Khedidja Mosbahi, Daniel Walker, Trevor Lithgow, Rhys Grinter

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
–field-weighted citation impact
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

34 citing papers in PubMed.

  1. Article
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  4. Article
  5. Review
  6. Article
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  9. Article
  10. POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Inokentijs JostsThe Hamburg Centre for Ultrafast Imaging (CUI), Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany; Department of Chemistry, Institute for Biochemistry and Molecular Biology, University of Hamburg, Martin-Luther-King-Platz 6, 20146 Hamburg, Germany.
Christopher James StubenrauchInfection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia.
Grishma VadlamaniInfection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia.
Khedidja MosbahiInstitute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
Daniel WalkerInstitute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow G12 8QQ, UK.
Trevor LithgowInfection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia.
Rhys GrinterInfection and Immunity Program, Biomedicine Discovery Institute and Department of Microbiology, Monash University, Melbourne, VIC 3804, Australia; Institute of Microbiology and Infection, School of Immunity and Infection, University of Birmingham, Birmingham B15 2TT, UK. Electronic address: rhys.grinter@monash.edu.

Funding

Wellcome TrustWellcome Trust 093592/Z/10/Z
6 · The paper itself

Abstract

The translocation and assembly module (TAM) plays a role in the transport and insertion of proteins into the bacterial outer membrane. TamB, a component of this system spans the periplasmic space to engage with its partner protein TamA. Despite efforts to characterize the TAM, the structure and mechanism of action of TamB remained enigmatic. Here we present the crystal structure of TamB amino acids 963-1,138. This region represents half of the conserved DUF490 domain, the defining feature of TamB. TamB

Indexed as

Conserved SequenceAmino Acid MotifsBacterial Outer Membrane ProteinsEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsProtein DomainsBacterial Outer Membrane ProteinsEscherichia coli ProteinschaperoneEscherichia colimembrane biologymicrobiologyprotein assemblyTamBX-ray crystallography

Identifiers

PMID29129383
PMCPMC5719984

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.