Evidence map›Paper›PMID 26919521›Full record

ArticleActa crystallographica. Section F, Structural biology communications2016

Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.

Kristin A Sutton, Jennifer Breen, Thomas A Russo, L Wayne Schultz, Timothy C Umland

Open access · bronzeAbstract read
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 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.9field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 18 citations in OpenAlex.

  1. Article
  2. Evolving dual-trait EPSP synthase variants using a synthetic yeast selection system.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Novel Coumarins Derivatives for A. baumannii Lung Infection Developed by High-Throughput Screening and Reinforcement Learning.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2024
    Article
  4. Targeting Shikimate Kinase Pathway ofJournal of tropical medicine · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Amino Acid Biosynthetic Pathways Are Required forAntimicrobial agents and chemotherapy · 2019
    Article
  10. Article
  11. Article
  12. 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

5 authors at 2 institutions in 1 country.

Kristin A SuttonHauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA.
Jennifer BreenHauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA.
Thomas A RussoDepartment of Medicine and The Witebsky Center for Microbial Pathogenesis, University at Buffalo, State University of New York, Buffalo, NY 14214, USA.
L Wayne SchultzHauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA.
Timothy C UmlandHauptman-Woodward Medical Research Institute, Buffalo, NY 14203, USA.
University at Buffalo, State University of New York · USHauptman-Woodward Medical Research Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzyme 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase catalyzes the sixth step of the seven-step shikimate pathway. Chorismate, the product of the pathway, is a precursor for the biosynthesis of aromatic amino acids, siderophores and metabolites such as folate, ubiquinone and vitamin K. The shikimate pathway is present in bacteria, fungi, algae, plants and apicomplexan parasites, but is absent in humans. The EPSP synthase enzyme produces 5-enolpyruvylshikimate 3-phosphate and phosphate from phosphoenolpyruvate and shikimate 3-phosphate via a transferase reaction, and is the target of the herbicide glyphosate. The Acinetobacter baumannii gene encoding EPSP synthase, aroA, has previously been demonstrated to be essential during host infection for the growth and survival of this clinically important drug-resistant ESKAPE pathogen. Prephenate dehydrogenase is also encoded by the bifunctional A. baumannii aroA gene, but its activity is dependent upon EPSP synthase since it operates downstream of the shikimate pathway. As part of an effort to evaluate new antimicrobial targets, recombinant A. baumannii EPSP (AbEPSP) synthase, comprising residues Ala301-Gln756 of the aroA gene product, was overexpressed in Escherichia coli, purified and crystallized. The crystal structure, determined to 2.37 Å resolution, is described in the context of a potential antimicrobial target and in comparison to EPSP synthases that are resistant or sensitive to the herbicide glyphosate.

Indexed as

3-Phosphoshikimate 1-CarboxyvinyltransferaseAcinetobacter baumanniiAmino Acid SequenceBacterial ProteinsCatalytic DomainCrystallizationCrystallography, X-RayModels, MolecularProtein Conformation, alpha-HelicalShikimic Acid3-Phosphoshikimate 1-CarboxyvinyltransferaseBacterial ProteinsShikimic Acidshikimic acid-3-phosphateAcinetobacter baumanniiantibiotic targetsEPSP synthaseessential genesmultidrug resistanceshikimate pathway

Identifiers

PMID26919521
PMCPMC4774876
OpenAlexW2275345627

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.