Evidence map›Paper›PMID 31205017›Full record

ArticleActa crystallographica. Section D, Structural biology2019

Analysis of crystalline and solution states of ligand-free spermidine N-acetyltransferase (SpeG) from Escherichia coli.

Ekaterina V Filippova, Steven Weigand, Olga Kiryukhina, Alan J Wolfe, Wayne F Anderson

Open access · bronzeAbstract read
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2019. 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
0.3field-weighted citation impact, top 41% 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, 9 citations in OpenAlex.

  1. Article
  2. 5-Thiohistidine N-Acetyltransferase from Proteiniphilum Saccharofermentans.Chembiochem : a European journal of chemical biology · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. GLO1 Contributes to the Drug Resistance ofInfection and drug resistance · 2022
    Article
  8. Article
  9. Criticality of a conserved tyrosine residue in the SpeG protein from Escherichia coli.Protein science : a publication of the Protein Society · 2021
    Article
  10. 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

5 authors at 3 institutions in 1 country.

Ekaterina V FilippovaCenter for Structural Genomics of Infectious Diseases, Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Steven WeigandDND-CAT Synchrotron Research Center, Argonne National Laboratory, Argonne, IL 60439, USA.
Olga KiryukhinaCenter for Structural Genomics of Infectious Diseases, Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Alan J WolfeDepartment of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago Health Sciences Division, Maywood, IL 60153, USA.ORCID 0000-0003-4532-0545
Wayne F AndersonCenter for Structural Genomics of Infectious Diseases, Department of Biochemistry and Molecular Genetics, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Northwestern University · USArgonne National Laboratory · USLoyola University Chicago · US

Funding

NIAID NIH HHS HHSN272200700058CNIAID NIH HHS HHSN272201200026CNIAID NIH HHS HHSN272201700060C
6 · The paper itself

Abstract

Spermidine N-acetyltransferase (SpeG) transfers an acetyl group from acetyl-coenzyme A to an N-terminal amino group of intracellular spermidine. This acetylation inactivates spermidine, reducing the polyamine toxicity that tends to occur under certain chemical and physical stresses. The structure of the SpeG protein from Vibrio cholerae has been characterized: while the monomer possesses a structural fold similar to those of other Gcn5-related N-acetyltransferase superfamily members, its dodecameric structure remains exceptional. In this paper, structural analyses of SpeG isolated from Escherichia coli are described. Like V. cholerae SpeG, E. coli SpeG forms dodecamers, as revealed by two crystal structures of the ligand-free E. coli SpeG dodecamer determined at 1.75 and 2.9 Å resolution. Although both V. cholerae SpeG and E. coli SpeG can adopt an asymmetric open dodecameric state, solution analysis showed that the oligomeric composition of ligand-free E. coli SpeG differs from that of ligand-free V. cholerae SpeG. Based on these data, it is proposed that the equilibrium balance of SpeG oligomers in the absence of ligands differs from one species to another and thus might be important for SpeG function.

Indexed as

Models, MolecularProtein Structure, QuaternaryAcetyltransferasesCrystallizationCrystallography, X-RayDiamine N-AcetyltransferaseEscherichia coli K12Escherichia coli ProteinsAcetyltransferasesDiamine N-AcetyltransferaseEscherichia coli ProteinsEscherichia coliGNAT familypolyamine acetylationSpeGspermidine N-acetyltransferase

Identifiers

PMID31205017
PMCPMC6580228
OpenAlexW2947035604

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.