Evidence map›Paper›PMID 29372903›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

Structure of aspartate β-semialdehyde dehydrogenase from Francisella tularensis.

N J Mank, S Pote, K A Majorek, A K Arnette, V G Klapper, B K Hurlburt, M Chruszcz

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

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. Taking biological structure communications into the third dimension.Acta crystallographica. Section F, Structural biology communications · 2019
    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

7 authors at 3 institutions in 1 country.

N J MankDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA.
S PoteDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA.
K A MajorekDepartment of Molecular Physiology and Biological Physics, University of Virginia, PO Box 800736, Charlottesville, VA 22908, USA.
A K ArnetteDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA.
V G KlapperDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA.
B K HurlburtAgricultural Research Service, Southern Regional Research Center, US Department of Agriculture, 1100 Robert E. Lee Boulevard, New Orleans, LA 70124, USA.
M ChruszczDepartment of Chemistry and Biochemistry, University of South Carolina, 631 Sumter Street, Columbia, SC 29208, USA.
University of South Carolina Sumter · USAgricultural Research Service · USUniversity of Virginia · US

Funding

U.S. Department of Energy, Biological and Environmental Research DE-AC02-06CH11357
6 · The paper itself

Abstract

Aspartate β-semialdehyde dehydrogenase (ASADH) is an enzyme involved in the diaminopimelate pathway of lysine biosynthesis. It is essential for the viability of many pathogenic bacteria and therefore has been the subject of considerable research for the generation of novel antibiotic compounds. This manuscript describes the first structure of ASADH from Francisella tularensis, the causative agent of tularemia and a potential bioterrorism agent. The structure was determined at 2.45 Å resolution and has a similar biological assembly to other bacterial homologs. ASADH is known to be dimeric in bacteria and have extensive interchain contacts, which are thought to create a half-sites reactivity enzyme. ASADH from higher organisms shows a tetrameric oligomerization, which also has implications for both reactivity and regulation. This work analyzes the apo form of F. tularensis ASADH, as well as the binding of the enzyme to its cofactor NADP

Indexed as

Amino Acid SequenceAspartate-Semialdehyde DehydrogenaseBacterial ProteinsCatalytic DomainCrystallography, X-RayFrancisella tularensisModels, MolecularNADPProtein Structure, QuaternaryRecombinant ProteinsSequence Homology, Amino AcidStructural Homology, ProteinAspartate-Semialdehyde DehydrogenaseBacterial ProteinsNADPRecombinant Proteinsamino-acid biosynthesisaspartate β-semialdehyde dehydrogenaseFrancisella tularensislysine biosynthesisoxidoreductasestularemia

Identifiers

PMID29372903
PMCPMC5947688
OpenAlexW2771569102

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.