Evidence map›Paper›PMID 25039253›Full record

ArticleThe FEBS journal2014

Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.

Izabela Sabala, Elzbieta Jagielska, Philip T Bardelang, Honorata Czapinska, Sven O Dahms, Jason A Sharpe, Richard James, Manuel E Than, Neil R Thomas, Matthias Bochtler

Open access · hybridAbstract read
In one paragraph

Article in The FEBS journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

51 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Peculiarities of the Interaction of the Bacteriolytic Protease Blp fromInternational journal of molecular sciences · 2026
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  15. Tracking Cell Wall-Anchored Proteins in Gram-Positive Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  16. Biomolecular NMR assignments · 2023
    Article
  17. Review
  18. Article
  19. Article
  20. Flourishing Antibacterial Strategies for Osteomyelitis Therapy.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    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

10 authors at 4 institutions in 3 countries.

Izabela SabalaInternational Institute of Molecular and Cell Biology, Warsaw, Poland.
Elzbieta Jagielska
Philip T Bardelang
Honorata Czapinska
Sven O Dahms
Jason A Sharpe
Richard James
Manuel E Than
Neil R Thomas
Matthias Bochtler
University of Nottingham · GBInternational Institute of Molecular and Cell Biology · PLLeibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DEInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

Medical Research Council
6 · The paper itself

Abstract

Staphylococcus simulans biovar staphylolyticus lysostaphin efficiently cleaves Staphylococcus aureus cell walls. The protein is in late clinical trials as a topical anti-staphylococcal agent, and can be used to prevent staphylococcal growth on artificial surfaces. Moreover, the gene has been both stably engineered into and virally delivered to mice or livestock to obtain resistance against staphylococci. Here, we report the first crystal structure of mature lysostaphin and two structures of its isolated catalytic domain at 3.5, 1.78 and 1.26 Å resolution, respectively. The structure of the mature active enzyme confirms its expected organization into catalytic and cell-wall-targeting domains. It also indicates that the domains are mobile with respect to each other because of the presence of a highly flexible peptide linker. The high-resolution structures of the catalytic domain provide details of Zn(2+) coordination and may serve as a starting point for the engineering of lysostaphin variants with improved biotechnological characteristics. STRUCTURED DIGITAL ABSTRACT: lysostaphin by x-ray crystallography (1, 2).

Indexed as

Bacterial ProteinsCatalytic DomainCoordination ComplexesCrystallography, X-RayLysostaphinModels, MolecularProtein Structure, SecondaryStaphylococcusZincBacterial ProteinsCoordination ComplexesLysostaphinZinccrystal structurelysislysostaphinStaphylococcus aureusStaphylococcus simulans

Identifiers

PMID25039253
PMCPMC4286107
OpenAlexW2140909578

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.