Evidence map›Paper›PMID 19194017›Full record

ArticleActa crystallographica. Section F, Structural biology and crystallization communications2009

Expression, purification, crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase from Bacillus anthracis in the presence of pyruvate.

Jarrod E Voss, Stephen W Scally, Nicole L Taylor, Con Dogovski, Malcolm R Alderton, Craig A Hutton, Juliet A Gerrard, Michael W Parker, Renwick C J Dobson, Matthew A Perugini

Open access · bronzeAbstract readComparative Study
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

10 citing papers in PubMed, 18 citations in OpenAlex.

  1. ColorimetricHeliyon · 2023
    Article
  2. Article
  3. Cloning to crystallization of dihydrodipicolinate synthase from the intracellular pathogen Legionella pneumophila.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013
    Article
  4. Article
  5. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the grapevine Vitis vinifera.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  6. Crystallization and preliminary X-ray diffraction analysis of dihydrodipicolinate synthase 2 from Arabidopsis thaliana.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011
    Article
  7. Cloning, expression, purification and crystallization of dihydrodipicolinate synthase from the psychrophile Shewanella benthica.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  8. Article
  9. Cloning, expression and crystallization of dihydrodipicolinate reductase from methicillin-resistant Staphylococcus aureus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    Article
  10. Crystallization and preliminary X-ray diffraction analysis of diaminopimelate epimerase from Escherichia coli.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010
    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

10 authors at 3 institutions in 2 countries.

Jarrod E VossDepartment of Biochemistry and Molecular Biology, University of Melbourne, Parkville, Victoria 3010, Australia.
Stephen W Scally
Nicole L Taylor
Con Dogovski
Malcolm R Alderton
Craig A Hutton
Juliet A Gerrard
Michael W Parker
Renwick C J Dobson
Matthew A Perugini
University of Melbourne · AUDefence Science and Technology Group · AUUniversity of Canterbury · NZ

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Dihydrodipicolinate synthase (DHDPS) catalyses the first committed step in the lysine-biosynthesis pathway in bacteria, plants and some fungi. In this study, the expression of DHDPS from Bacillus anthracis (Ba-DHDPS) and the purification of the recombinant enzyme in the absence and presence of the substrate pyruvate are described. It is shown that DHDPS from B. anthracis purified in the presence of pyruvate yields greater amounts of recombinant enzyme with more than 20-fold greater specific activity compared with the enzyme purified in the absence of substrate. It was therefore sought to crystallize Ba-DHDPS in the presence of the substrate. Pyruvate was soaked into crystals of Ba-DHDPS prepared in 0.2 M sodium fluoride, 20%(w/v) PEG 3350 and 0.1 M bis-tris propane pH 8.0. Preliminary X-ray diffraction data of the recombinant enzyme soaked with pyruvate at a resolution of 2.15 A are presented. The pending crystal structure of the pyruvate-bound form of Ba-DHDPS will provide insight into the function and stability of this essential bacterial enzyme.

Indexed as

X-Ray DiffractionBacillus anthracisCrystallizationGene Expression Regulation, BacterialHydro-LyasesIsoenzymesPyruvic AcidSubstrate Specificity4-hydroxy-tetrahydrodipicolinate synthaseHydro-LyasesIsoenzymesPyruvic Acid

Identifiers

PMID19194017
PMCPMC2635873
OpenAlexW2009191531

What OpenQuestion holds

Textmetadata
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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.