Evidence map›Paper›PMID 17994105›Full record

ArticleNature structural & molecular biology2007

Autotransporter structure reveals intra-barrel cleavage followed by conformational changes.

Travis J Barnard, Nathalie Dautin, Petra Lukacik, Harris D Bernstein, Susan K Buchanan

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed, 1 pooled it
8.2field-weighted citation impact, top 2% 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

88 citing papers in PubMed, 1 synthesis or guideline pooled it, 163 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021
    Review
  11. Article
  12. Article
  13. Article
  14. Properties of protein unfolded states suggest broad selection for expanded conformational ensembles.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. BamA is required for autotransporter secretion.Biochimica et biophysica acta. General subjects · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

28 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

5 authors at 2 institutions in 1 country.

Travis J BarnardLaboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, US National Institutes of Health, Bethesda, Maryland 20892, USA.
Nathalie Dautin
Petra Lukacik
Harris D Bernstein
Susan K Buchanan
National Institute of Diabetes and Digestive and Kidney Diseases · USNational Institutes of Health · US

Funding

Biogenesis of bacterial autotransporter proteinsZ01DK052037 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BERNSTEIN, HARRIS · 2007 to 2008
$906k
structural characterization of bacterial secretion channelsZ01DK036139 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BUCHANAN, SUSAN · 2007 to 2008
$726k
Intramural NIH HHS Z01 DK036139
6 · The paper itself

Abstract

Autotransporters are virulence factors produced by Gram-negative bacteria. They consist of two domains, an N-terminal 'passenger' domain and a C-terminal beta-domain. beta-domains form beta-barrel structures in the outer membrane while passenger domains are translocated into the extracellular space. In some autotransporters, the two domains are separated by proteolytic cleavage. Using X-ray crystallography, we solved the 2.7-A structure of the post-cleavage state of the beta-domain of EspP, an autotransporter produced by Escherichia coli strain O157:H7. The structure consists of a 12-stranded beta-barrel with the passenger domain-beta-domain cleavage junction located inside the barrel pore, approximately midway between the extracellular and periplasmic surfaces of the outer membrane. The structure reveals an unprecedented intra-barrel cleavage mechanism and suggests that two conformational changes occur in the beta-domain after cleavage, one conferring increased stability on the beta-domain and another restricting access to the barrel pore.

Indexed as

Crystallography, X-RayEscherichia coli O157Escherichia coli ProteinsHydrolysisPoint MutationProtein ConformationSerine EndopeptidasesStatic ElectricityEscherichia coli ProteinsEspP protein, E coliSerine Endopeptidases

Identifiers

PMID17994105
PMCPMC2551741
OpenAlexW1991736406

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.