Evidence map›Paper›PMID 31750992›Full record

ArticleThe FEBS journal2020

Structural and biochemical analysis of Bacillus anthracis prephenate dehydrogenase reveals an unusual mode of inhibition by tyrosine via the ACT domain.

Ivan G Shabalin, Artyom Gritsunov, Jing Hou, Joanna Sławek, Charles D Miks, David R Cooper, Wladek Minor, Dinesh Christendat

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

Article in The FEBS journal, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 54% 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

1 citing paper in PubMed, 6 citations in OpenAlex.

  1. Intragenic suppressors unravel the role of the SCREAM ACT-like domain for bHLH partner selectivity in stomatal development.Proceedings of the National Academy of Sciences of the United States of America · 2022
    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 4 institutions in 3 countries.

Ivan G ShabalinDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0003-3955-9242
Artyom GritsunovDepartment of Cell and Systems Biology, University of Toronto, ON, Canada.ORCID 0000-0002-6152-6175
Jing HouDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-5520-9237
Joanna SławekDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-1754-2741
Charles D MiksDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0002-7463-5127
David R CooperDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0001-5240-9789
Wladek MinorDepartment of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA, USA.ORCID 0000-0001-7075-7090
Dinesh ChristendatDepartment of Cell and Systems Biology, University of Toronto, ON, Canada.ORCID 0000-0002-2919-3534
Joint Center for Structural Genomics · USUniversity of Toronto · CAJagiellonian University · PLUniversity of Virginia · US

Funding

Reproducible, Unbiased Ligand Identification Assisted by Artificial Intelligence and Development of Ligand Reference LibrariesR01GM132595 · NIGMS · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2019 to 2022
$2.3M
Metal binding sites in macromolecular structuresR01GM117325 · NIGMS · UNIVERSITY OF VIRGINIA · PI MINOR, WLADEK · 2016 to 2019
$1.3M
Accurate measurements of phasing signal to determine macromolecular structuresR01GM118619 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI OTWINOWSKI, ZBYSZEK · 2017 to 2020
$1.3M
NIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060CNIGMS NIH HHS R01 GM117325NIGMS NIH HHS R01 GM118619NIGMS NIH HHS R01 GM132595
6 · The paper itself

Abstract

Tyrosine biosynthesis via the shikimate pathway is absent in humans and other animals, making it an attractive target for next-generation antibiotics, which is increasingly important due to the looming proliferation of multidrug-resistant pathogens. Tyrosine biosynthesis is also of commercial importance for the environmentally friendly production of numerous compounds, such as pharmaceuticals, opioids, aromatic polymers, and petrochemical aromatics. Prephenate dehydrogenase (PDH) catalyzes the penultimate step of tyrosine biosynthesis in bacteria: the oxidative decarboxylation of prephenate to 4-hydroxyphenylpyruvate. The majority of PDHs are competitively inhibited by tyrosine and consist of a nucleotide-binding domain and a dimerization domain. Certain PDHs, including several from pathogens on the World Health Organization priority list of antibiotic-resistant bacteria, possess an additional ACT domain. However, biochemical and structural knowledge was lacking for these enzymes. In this study, we successfully established a recombinant protein expression system for PDH from Bacillus anthracis (BaPDH), the causative agent of anthrax, and determined the structure of a BaPDH ternary complex with NAD

Indexed as

Bacillus anthracisCatalysisCatalytic DomainCrystallography, X-RayCyclohexanecarboxylic AcidsCyclohexenesHumansPrephenate DehydrogenaseProtein DomainsTyrosineCyclohexanecarboxylic AcidsCyclohexenesPrephenate Dehydrogenaseprephenic acidTyrosineACT domainallosteric regulationBacillus anthracisprephenate dehydrogenasetyrosine biosynthesis

Identifiers

PMID31750992
PMCPMC7239764
OpenAlexW2990971204

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.