Evidence map›Paper›PMID 33574254›Full record

ArticleNature communications2021

Mechanisms of feedback inhibition and sequential firing of active sites in plant aspartate transcarbamoylase.

Leo Bellin, Francisco Del Caño-Ochoa, Adrián Velázquez-Campoy, Torsten Möhlmann, Santiago Ramón-Maiques

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 28 citations in OpenAlex.

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  14. New Insight into Aspartate Metabolic Pathways inInternational journal of molecular sciences · 2022
    Article
  15. Cytidine Triphosphate Synthase Four FromFrontiers in plant science · 2022
    Article
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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 4 institutions in 2 countries.

Leo BellinPflanzenphysiologie, Fachbereich Biologie, Universität Kaiserslautern, Erwin-Schrödinger-Strasse, D-67663, Kaiserslautern, Germany.ORCID 0000-0002-6003-2931
Francisco Del Caño-OchoaInstituto de Biomedicina de Valencia (IBV-CSIC), Jaime Roig 11, 46010, Valencia, Spain.ORCID 0000-0003-3093-3103
Adrián Velázquez-CampoyInstitute for Biocomputation and Physics of Complex Systems (BIFI), Joint Units IQFR-CSIC-BIFI, and GBsC-CSIC-BIFI, Universidad de Zaragoza, 50018, Zaragoza, Spain.ORCID 0000-0001-5702-4538
Torsten MöhlmannPflanzenphysiologie, Fachbereich Biologie, Universität Kaiserslautern, Erwin-Schrödinger-Strasse, D-67663, Kaiserslautern, Germany. moehlmann@biologie.uni-kl.de.ORCID 0000-0002-5676-2042
Santiago Ramón-MaiquesInstituto de Biomedicina de Valencia (IBV-CSIC), Jaime Roig 11, 46010, Valencia, Spain. sramon@ibv.csic.es.ORCID 0000-0001-9674-8088
University of Kaiserslautern · DECentro de Investigación Biomédica en Red · ESInstituto de Biomedicina de Valencia · ESUniversidad de Zaragoza · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aspartate transcarbamoylase (ATC), an essential enzyme for de novo pyrimidine biosynthesis, is uniquely regulated in plants by feedback inhibition of uridine 5-monophosphate (UMP). Despite its importance in plant growth, the structure of this UMP-controlled ATC and the regulatory mechanism remain unknown. Here, we report the crystal structures of Arabidopsis ATC trimer free and bound to UMP, complexed to a transition-state analog or bearing a mutation that turns the enzyme insensitive to UMP. We found that UMP binds and blocks the ATC active site, directly competing with the binding of the substrates. We also prove that UMP recognition relies on a loop exclusively conserved in plants that is also responsible for the sequential firing of the active sites. In this work, we describe unique regulatory and catalytic properties of plant ATCs that could be exploited to modulate de novo pyrimidine synthesis and plant growth.

Indexed as

ArabidopsisAspartate CarbamoyltransferaseAspartic AcidBinding SitesCatalytic DomainFeedbackModels, MolecularProtein ConformationPyrimidinesUridine MonophosphateAspartate CarbamoyltransferaseAspartic AcidpyrimidinePyrimidinesUridine Monophosphate

Identifiers

PMID33574254
PMCPMC7878868
OpenAlexW3128928809

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.