Evidence map›Paper›PMID 27917836›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

The crystal structure of dihydrodipicolinate reductase from the human-pathogenic bacterium Bartonella henselae strain Houston-1 at 2.3 Å resolution.

Ali R Cala, Maria T Nadeau, Jan Abendroth, Bart L Staker, Alexandra R Reers, Anthony W Weatherhead, Renwick C J Dobson, Peter J Myler, André O Hudson

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

Article in Acta crystallographica. Section F, Structural biology communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. 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

9 authors at 8 institutions in 3 countries.

Ali R CalaThomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, 85 Lomb Memorial Drive, Rochester, NY 14623-5603, USA.
Maria T NadeauSchool of Chemistry and Materials Science, Rochester Institute of Technology, 85 Lomb Memorial Drive, Rochester, NY 14623-5603, USA.
Jan AbendrothBeryllium Discovery Inc., Bainbridge Island, WA 98110, USA.
Bart L StakerSeattle Structural Genomics Center for Infectious Disease, USA.
Alexandra R ReersSeattle Structural Genomics Center for Infectious Disease, USA.
Anthony W WeatherheadBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, New Zealand.
Renwick C J DobsonBiomolecular Interaction Centre, School of Biological Sciences, University of Canterbury, Private Bag 4800, Christchurch, New Zealand.
Peter J MylerSeattle Structural Genomics Center for Infectious Disease, USA.
André O HudsonThomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, 85 Lomb Memorial Drive, Rochester, NY 14623-5603, USA.
Rochester Institute of Technology · USBeryllium (United States) · USCenter for Infectious Disease Research · USInfectious Disease Research Institute · USLos Alamos National Laboratory · USUniversity of Canterbury · NZUniversity of Melbourne · AUUniversity of Washington · US

Funding

Genetic and structural analysis of L,L-diaminopimelate aminotransferase (DapL): An attractive target for the development of narrow-spectrum antibioticsR15GM120653 · NIGMS · ROCHESTER INSTITUTE OF TECHNOLOGY · PI HUDSON, ANDRE O · 2016 to 2017
$468k
NIGMS NIH HHS R15 GM120653
6 · The paper itself

Abstract

In bacteria, the second committed step in the diaminopimelate/lysine anabolic pathways is catalyzed by the enzyme dihydrodipicolinate reductase (DapB). DapB catalyzes the reduction of dihydrodipicolinate to yield tetrahydrodipicolinate. Here, the cloning, expression, purification, crystallization and X-ray diffraction analysis of DapB from the human-pathogenic bacterium Bartonella henselae, the causative bacterium of cat-scratch disease, are reported. Protein crystals were grown in conditions consisting of 5%(w/v) PEG 4000, 200 mM sodium acetate, 100 mM sodium citrate tribasic pH 5.5 and were shown to diffract to ∼2.3 Å resolution. They belonged to space group P4

Indexed as

Amino Acid SequenceBacterial ProteinsBartonella henselaeBinding SitesCloning, MolecularCrystallography, X-RayDihydrodipicolinate ReductaseEscherichia coliGene ExpressionModels, MolecularNADPPlasmidsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsBacterial ProteinsDihydrodipicolinate ReductaseNADPRecombinant ProteinsBartonella henselaecat-scratch diseasediaminopimelatedihydrodipicolinate reductaselysine biosynthesis

Identifiers

PMID27917836
PMCPMC5137465
OpenAlexW2552306121

What OpenQuestion holds

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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.