Evidence map›Paper›PMID 28646214›Full record

ArticleScientific reports2017

Structural and biochemical studies of sulphotransferase 18 from Arabidopsis thaliana explain its substrate specificity and reaction mechanism.

Felix Hirschmann, Florian Krause, Petra Baruch, Igor Chizhov, Jonathan Wolf Mueller, Dietmar J Manstein, Jutta Papenbrock, Roman Fedorov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Sulfation pathways from red to green.The Journal of biological chemistry · 2019
    Review
  18. Review
  19. 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 3 institutions in 2 countries.

Felix HirschmannInstitute of Botany, Leibniz University Hannover, Herrenhäuserstr. 2, D-30419, Hannover, Germany.
Florian KrauseInstitute of Botany, Leibniz University Hannover, Herrenhäuserstr. 2, D-30419, Hannover, Germany.
Petra BaruchInstitute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625, Hannover, Germany.
Igor ChizhovInstitute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625, Hannover, Germany.
Jonathan Wolf MuellerInstitute of Metabolism and Systems Research (IMSR), University of Birmingham, Birmingham, B15 2TT, UK.ORCID 0000-0003-1212-189X
Dietmar J MansteinInstitute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625, Hannover, Germany.ORCID 0000-0003-0763-0147
Jutta PapenbrockInstitute of Botany, Leibniz University Hannover, Herrenhäuserstr. 2, D-30419, Hannover, Germany. Jutta.Papenbrock@botanik.uni-hannover.de.
Roman FedorovInstitute for Biophysical Chemistry, Hannover Medical School, Carl-Neuberg-Strasse 1, D-30625, Hannover, Germany. Fedorov.Roman@mh-hannover.de.
Medizinische Hochschule Hannover · DELeibniz University Hannover · DEBirmingham City University · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sulphotransferases are a diverse group of enzymes catalysing the transfer of a sulfuryl group from 3'-phosphoadenosine 5'-phosphosulphate (PAPS) to a broad range of secondary metabolites. They exist in all kingdoms of life. In Arabidopsis thaliana (L.) Heynh. twenty-two sulphotransferase (SOT) isoforms were identified. Three of those are involved in glucosinolate (Gl) biosynthesis, glycosylated sulphur-containing aldoximes containing chemically different side chains, whose break-down products are involved in stress response against herbivores, pathogens, and abiotic stress. To explain the differences in substrate specificity of desulpho (ds)-Gl SOTs and to understand the reaction mechanism of plant SOTs, we determined the first high-resolution crystal structure of the plant ds-Gl SOT AtSOT18 in complex with 3'-phosphoadenosine 5'-phosphate (PAP) alone and together with the Gl sinigrin. These new structural insights into the determination of substrate specificity were complemented by mutagenesis studies. The structure of AtSOT18 invigorates the similarity between plant and mammalian sulphotransferases, which illustrates the evolutionary conservation of this multifunctional enzyme family. We identified the essential residues for substrate binding and catalysis and demonstrated that the catalytic mechanism is conserved between human and plant enzymes. Our study indicates that the loop-gating mechanism is likely to be a source of the substrate specificity in plants.

Indexed as

Adenosine DiphosphateAmino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesBiocatalysisCrystallography, X-RayDNA Mutational AnalysisGlucosinolatesKineticsLigandsModels, BiologicalMutagenesisSubstrate SpecificitySulfotransferasesadenosine 3'-phosphate-5'-phosphateAdenosine DiphosphateArabidopsis ProteinsGlucosinolatesLigandssinigrinSOT18 protein, ArabidopsisSulfotransferases

Identifiers

PMID28646214
PMCPMC5482895
OpenAlexW2657020888

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.