Evidence map›Paper›PMID 23819763›Full record

ArticleJournal of the American Chemical Society2013

Reaction products and the X-ray structure of AmpDh2, a virulence determinant of Pseudomonas aeruginosa.

Siseth Martínez-Caballero, Mijoon Lee, Cecilia Artola-Recolons, César Carrasco-López, Dusan Hesek, Edward Spink, Elena Lastochkin, Weilie Zhang, Lance M Hellman, Bill Boggess and 2 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. 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
–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

27 citing papers in PubMed.

  1. Article
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  8. Integrative structural biology of the penicillin-binding protein-1 fromComputational and structural biotechnology journal · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Review
  14. Lytic transglycosylases: concinnity in concision of the bacterial cell wall.Critical reviews in biochemistry and molecular biology · 2017
    Review
  15. Deciphering the Nature of Enzymatic Modifications of Bacterial Cell Walls.Chembiochem : a European journal of chemical biology · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. 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

12 authors.

Siseth Martínez-Caballero *Department of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC, Serrano 119, 28006 Madrid, Spain.
Mijoon Lee *Department of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Cecilia Artola-Recolons *Department of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC, Serrano 119, 28006 Madrid, Spain.
César Carrasco-LópezDepartment of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC, Serrano 119, 28006 Madrid, Spain.
Dusan HesekDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Edward SpinkDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Elena LastochkinDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Weilie ZhangDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Lance M HellmanDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Bill BoggessDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Shahriar MobasheryDepartment of Chemistry and Biochemistry, Nieuwland Science Hall, Notre Dame, Indiana 46556, United States.
Juan A HermosoDepartment of Crystallography and Structural Biology, Inst. Química-Física "Rocasolano", CSIC, Serrano 119, 28006 Madrid, Spain.

Funding

Penicillin-Binding Proteins, Mechanism and InhibitionR01GM061629 · NIGMS · WAYNE STATE UNIVERSITY · PI MOBASHERY, SHAHRIAR · 2001 to 2018
$5.1M
NIGMS NIH HHS GM61629NIGMS NIH HHS R01 GM061629
6 · The paper itself

Abstract

The zinc protease AmpDh2 is a virulence determinant of Pseudomonas aeruginosa, a problematic human pathogen. The mechanism of how the protease manifests virulence is not known, but it is known that it turns over the bacterial cell wall. The reaction of AmpDh2 with the cell wall was investigated, and nine distinct turnover products were characterized by LC/MS/MS. The enzyme turns over both the cross-linked and noncross-linked cell wall. Three high-resolution X-ray structures, the apo enzyme and two complexes with turnover products, were solved. The X-ray structures show how the dimeric protein interacts with the inner leaflet of the bacterial outer membrane and that the two monomers provide a more expansive surface for recognition of the cell wall. This binding surface can accommodate the 3D solution structure of the cross-linked cell wall.

Indexed as

Bacterial ProteinsCrystallography, X-RayMetalloproteasesModels, MolecularMolecular ConformationMolecular StructurePseudomonas aeruginosaVirulence FactorsAmpDh2 protein, Pseudomonas aeruginosaBacterial ProteinsMetalloproteasesVirulence Factors

Identifiers

PMID23819763
PMCPMC3775653

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Registered trials

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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.