Evidence map›Paper›PMID 21612658›Full record

ArticleBMC microbiology2011

The crystal structure of alanine racemase from Streptococcus pneumoniae, a target for structure-based drug design.

Hookang Im, Miriam L Sharpe, Ulrich Strych, Milya Davlieva, Kurt L Krause

Open access · goldAbstract read
In one paragraph

Article in BMC microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. BioMed research international · 2024
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  3. Article
  4. International journal of molecular sciences · 2023
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  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The structure of alanine racemase from Acinetobacter baumannii.Acta crystallographica. Section F, Structural biology communications · 2014
    Article
  11. Article
  12. Article
  13. Crystallization and preliminary X-ray study of a thermostable alanine racemase from Thermoanaerobacter tengcongensis MB4.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  14. Article
  15. Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  16. Article
  17. Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).Acta crystallographica. Section D, Biological crystallography · 2012
    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

5 authors at 3 institutions in 3 countries.

Hookang ImResearch Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul, Korea.
Miriam L Sharpe
Ulrich Strych
Milya Davlieva
Kurt L Krause
University of Otago · NZRice University · USSeoul National University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStreptococcus pneumoniae is a globally important pathogen. The Gram-positive diplococcus is a leading cause of pneumonia, otitis media, bacteremia, and meningitis, and antibiotic resistant strains have become increasingly common over recent years. Alanine racemase is a ubiquitous enzyme among bacteria and provides the essential cell wall precursor, D-alanine. Since it is absent in humans, this enzyme is an attractive target for the development of drugs against S. pneumoniae and other bacterial pathogens.

resultsHere we report the crystal structure of alanine racemase from S. pneumoniae (AlrSP). Crystals diffracted to a resolution of 2.0 Å and belong to the space group P3121 with the unit cell parameters a = b = 119.97 Å, c = 118.10 Å, α = β = 90° and γ = 120°. Structural comparisons show that AlrSP shares both an overall fold and key active site residues with other bacterial alanine racemases. The active site cavity is similar to other Gram positive alanine racemases, featuring a restricted but conserved entryway.

conclusionsWe have solved the structure of AlrSP, an essential step towards the development of an accurate pharmacophore model of the enzyme, and an important contribution towards our on-going alanine racemase structure-based drug design project. We have identified three regions on the enzyme that could be targeted for inhibitor design, the active site, the dimer interface, and the active site entryway.

Indexed as

Alanine RacemaseAmino Acid SequenceCatalytic DomainCrystallography, X-RayDrug DesignHumansModels, MolecularMolecular Sequence DataProtein MultimerizationProtein Structure, QuaternaryProtein Structure, TertiarySequence Homology, Amino AcidStreptococcus pneumoniaeAlanine Racemase

Identifiers

PMID21612658
PMCPMC3146814
OpenAlexW2084010248

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LicenceCC BY
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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.