Evidence map›Paper›PMID 31860061›Full record

ArticleBioscience reports2020

Insights into the Cnx1E catalyzed MPT-AMP hydrolysis.

Thomas W Hercher, Joern Krausze, Sven Hoffmeister, Dagmar Zwerschke, Thomas Lindel, Wulf Blankenfeldt, Ralf R Mendel, Tobias Kruse

Open access · goldAbstract read
In one paragraph

Article in Bioscience reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 33% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. The structural principles underlying molybdenum insertase complex assembly.Protein science : a publication of the Protein Society · 2023
    Article
  6. Function of Molybdenum Insertases.Molecules (Basel, Switzerland) · 2022
    Review
  7. The History of the Molybdenum Cofactor-A Personal View.Molecules (Basel, Switzerland) · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Biological pincer complexes.ChemCatChem · 2020
    Article
  13. The structure of the Moco carrier protein from Rippkaea orientalis.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  14. The First Step ofMicroorganisms · 2020
    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 2 institutions in 1 country.

Thomas W HercherTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Joern KrauszeTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Sven HoffmeisterTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Dagmar ZwerschkeTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Thomas LindelTU Braunschweig, Institute of Organic Chemistry, Hagenring 30, 38106 Braunschweig, Germany.
Wulf BlankenfeldtStructure and Function of Proteins, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124 Braunschweig, Germany.
Ralf R MendelTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Tobias KruseTU Braunschweig, Institute of Plant Biology, Spielmannstrasse 7, 38106 Braunschweig, Germany.
Technische Universität Braunschweig · DEHelmholtz Centre for Infection Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Molybdenum insertases (Mo-insertases) catalyze the final step of molybdenum cofactor (Moco) biosynthesis, an evolutionary old and highly conserved multi-step pathway. In the first step of the pathway, GTP serves as substrate for the formation of cyclic pyranopterin monophosphate, which is subsequently converted into molybdopterin (MPT) in the second pathway step. In the following synthesis steps, MPT is adenylated yielding MPT-AMP that is subsequently used as substrate for enzyme catalyzed molybdate insertion. Molybdate insertion and MPT-AMP hydrolysis are catalyzed by the Mo-insertase E-domain. Earlier work reported a highly conserved aspartate residue to be essential for Mo-insertase functionality. In this work, we confirmed the mechanistic relevance of this residue for the Arabidopsis thaliana Mo-insertase Cnx1E. We found that the conservative substitution of Cnx1E residue Asp274 by Glu (D274E) leads to an arrest of MPT-AMP hydrolysis and hence to the accumulation of MPT-AMP. We further showed that the MPT-AMP accumulation goes in hand with the accumulation of molybdate. By crystallization and structure determination of the Cnx1E variant D274E, we identified the potential reason for the missing hydrolysis activity in the disorder of the region spanning amino acids 269 to 274. We reasoned that this is caused by the inability of a glutamate in position 274 to coordinate the octahedral Mg2+-water complex in the Cnx1E active site.

Indexed as

Adenosine MonophosphateAmino AcidsAmino Acid SequenceArabidopsisArabidopsis ProteinsCatalysisCatalytic DomainCoenzymesHydrolysisMetalloproteinsMolybdenumMolybdenum CofactorsOrganophosphorus CompoundsPteridinesPterinsAdenosine MonophosphateAmino AcidsArabidopsis ProteinsCoenzymesMetalloproteinsmolybdateMolybdenumMolybdenum CofactorsmolybdopterinnulibryOrganophosphorus CompoundsPteridinesPterinsAdenylated molybdopterinEnzyme catalyzed hydrolysisMolybdenum cofactorMolybdenum insertase

Identifiers

PMID31860061
PMCPMC6954367
OpenAlexW3000695858

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.