Evidence map›Paper›PMID 18453697›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008

Structures of an alanine racemase from Bacillus anthracis (BA0252) in the presence and absence of (R)-1-aminoethylphosphonic acid (L-Ala-P).

Kinfai Au, Jingshan Ren, Thomas S Walter, Karl Harlos, Joanne E Nettleship, Raymond J Owens, David I Stuart, Robert M Esnouf

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. 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
  6. Crystallization and preliminary X-ray diffraction analysis of alanine racemase from Pseudomonas putida YZ-26.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012
    Article
  7. Structural features and kinetic characterization of alanine racemase from Staphylococcus aureus (Mu50).Acta crystallographica. Section D, Biological crystallography · 2012
    Article
  8. Article
  9. Article
  10. (R)-(1-Ammonio-eth-yl)phospho-nate.Acta crystallographica. Section E, Structure reports online · 2010
    Article
  11. Structure of the Escherichia coli RNA polymerase alpha subunit C-terminal domain.Acta crystallographica. Section D, Biological crystallography · 2010
    Article
  12. Article
  13. 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 2 institutions in 1 country.

Kinfai AuOxford Protein Production Facility, The Henry Wellcome Building for Genomic Medicine, Oxford University, Roosevelt Drive, Oxford OX3 7BN, England.
Jingshan Ren
Thomas S Walter
Karl Harlos
Joanne E Nettleship
Raymond J Owens
David I Stuart
Robert M Esnouf
Centre for Human Genetics · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council G0400717
6 · The paper itself

Abstract

Bacillus anthracis, the causative agent of anthrax, has been targeted by the Oxford Protein Production Facility to validate high-throughput protocols within the Structural Proteomics in Europe project. As part of this work, the structures of an alanine racemase (BA0252) in the presence and absence of the inhibitor (R)-1-aminoethylphosphonic acid (L-Ala-P) have determined by X-ray crystallography to resolutions of 2.1 and 1.47 A, respectively. Difficulties in crystallizing this protein were overcome by the use of reductive methylation. Alanine racemase has attracted much interest as a possible target for anti-anthrax drugs: not only is D-alanine a vital component of the bacterial cell wall, but recent studies also indicate that alanine racemase, which is accessible in the exosporium, plays a key role in inhibition of germination in B. anthracis. These structures confirm the binding mode of L-Ala-P but suggest an unexpected mechanism of inhibition of alanine racemase by this compound and could provide a basis for the design of improved alanine racemase inhibitors with potential as anti-anthrax therapies.

Indexed as

Alanine RacemaseAmino Acid SequenceAminoethylphosphonic AcidBacillus anthracisBinding SitesCrystallography, X-RayMethylationMolecular Sequence DataMolecular StructureProtein ConformationSequence Homology, Amino AcidStereoisomerismAlanine RacemaseAminoethylphosphonic Acid

Identifiers

PMID18453697
PMCPMC2376406
OpenAlexW2027132083

What OpenQuestion holds

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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.