Evidence map›Paper›PMID 25605729›Full record

ArticleThe Journal of biological chemistry2015

Structural and biochemical analysis of the essential diadenylate cyclase CdaA from Listeria monocytogenes.

Jonathan Rosenberg, Achim Dickmanns, Piotr Neumann, Katrin Gunka, Johannes Arens, Volkhard Kaever, Jörg Stülke, Ralf Ficner, Fabian M Commichau

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
8.5field-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

44 citing papers in PubMed, 79 citations in OpenAlex.

  1. Review
  2. TheInfection and immunity · 2026
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  7. Crystallographic fragment screen of the c-di-AMP-synthesizing enzyme CdaA from Bacillus subtilis.Acta crystallographica. Section F, Structural biology communications · 2024
    Article
  8. Article
  9. Article
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  11. Cyclic di-AMP traps proton-coupled KNature communications · 2023
    Article
  12. Review
  13. C-di-AMP Is a Second Messenger inMicroorganisms · 2023
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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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 1 institution in 1 country.

Jonathan RosenbergFrom the Departments of General Microbiology and.
Achim DickmannsMolecular Structural Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen, D-37077 Göttingen, Germany and.
Piotr NeumannMolecular Structural Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen, D-37077 Göttingen, Germany and.
Katrin GunkaFrom the Departments of General Microbiology and.
Johannes ArensMolecular Structural Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen, D-37077 Göttingen, Germany and.
Volkhard Kaeverthe Research Core Unit Metabolomics, Hannover Medical School, D-30625 Hannover, Germany.
Jörg StülkeFrom the Departments of General Microbiology and.
Ralf FicnerMolecular Structural Biology, Institute for Microbiology and Genetics, Georg-August University Göttingen, D-37077 Göttingen, Germany and.
Fabian M CommichauFrom the Departments of General Microbiology and fcommic1@gwdg.de.
General Department of Preventive Medicine · VN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The recently identified second messenger cyclic di-AMP (c-di-AMP) is involved in several important cellular processes, such as cell wall metabolism, maintenance of DNA integrity, ion transport, transcription regulation, and allosteric regulation of enzyme function. Interestingly, c-di-AMP is essential for growth of the Gram-positive model bacterium Bacillus subtilis. Although the genome of B. subtilis encodes three c-di-AMP-producing diadenlyate cyclases that can functionally replace each other, the phylogenetically related human pathogens like Listeria monocytogenes and Staphylococcus aureus possess only one enzyme, the diadenlyate cyclase CdaA. Because CdaA is also essential for growth of these bacteria, the enzyme is a promising target for the development of novel antibiotics. Here we present the first crystal structure of the L. monocytogenes CdaA diadenylate cyclase domain that is conserved in many human pathogens. Moreover, biochemical characterization of the cyclase revealed an unusual metal cofactor requirement.

Indexed as

Crystallography, X-RayAmino Acid SequenceBacillus subtilisBacterial ProteinsCatalysisCell WallCobaltDinucleoside PhosphatesHumansListeria monocytogenesPhosphorus-Oxygen LyasesProtein ConformationBacterial ProteinsCobaltcyclic diadenosine phosphatediadenylate cyclase, Bacillus subtilisDinucleoside PhosphatesPhosphorus-Oxygen LyasesBacterial Signal TransductionCrystal StructureCyclic Diadenosine Monophosphate (c-di-AMP)Enzyme CatalysisSecond Messenger

Identifiers

PMID25605729
PMCPMC4358292
OpenAlexW1977663621

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.