Evidence map›Paper›PMID 21167155›Full record

ArticleFEBS letters2011

Recognition of peptidoglycan and β-lactam antibiotics by the extracellular domain of the Ser/Thr protein kinase StkP from Streptococcus pneumoniae.

Beatriz Maestro, Linda Novaková, Dusan Hesek, Mijoon Lee, Eduardo Leyva, Shahriar Mobashery, Jesús M Sanz, Pavel Branny

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

38 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
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  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Integrative structural biology of the penicillin-binding protein-1 fromComputational and structural biotechnology journal · 2021
    Article
  13. The PASTA domains ofMicrobiology (Reading, England) · 2020
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Phosphorylation-dependent activation of the cell wall synthase PBP2a inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  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

8 authors at 3 institutions in 3 countries.

Beatriz MaestroInstituto de Biologia Molecular y Celular, Universidad Miguel Hernández, Elche, Spain.
Linda Novaková
Dusan Hesek
Mijoon Lee
Eduardo Leyva
Shahriar Mobashery
Jesús M Sanz
Pavel Branny
Universitat de Miguel Hernández d'Elx · ESUniversity of Notre Dame · USCzech Academy of Sciences, Institute of Microbiology · CZ

Funding

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

Abstract

The eukaryotic-type serine/threonine kinase StkP from Streptococcus pneumoniae is an important signal-transduction element that regulates the expression of numerous pneumococcal genes. We have expressed the extracellular C-terminal domain of StkP kinase (C-StkP), elaborated a three-dimensional structural model and performed a spectroscopical characterization of its structure and stability. Biophysical experiments show that C-StkP binds to synthetic samples of the cell wall peptidoglycan (PGN) and to β-lactam antibiotics, which mimic the terminal portions of the PGN stem peptide. This is the first experimental report on the recognition of a minimal PGN unit by a PASTA-containing kinase, suggesting that non-crosslinked PGN may act as a signal for StkP function and pointing to this protein as an interesting target for β-lactam antibiotics.

Indexed as

Protein Interaction Domains and MotifsAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsBinding SitesCell WallModels, MolecularPeptidoglycanProtein BindingProtein Serine-Threonine KinasesSpectrum AnalysisStreptococcus pneumoniaeAnti-Bacterial AgentsBacterial Proteinsbeta-LactamsPeptidoglycanProtein Serine-Threonine Kinases

Identifiers

PMID21167155
PMCPMC3035916
OpenAlexW2084315238

What OpenQuestion holds

Textmetadata
LicenceTDM
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.