Evidence map›Paper›PMID 32057875›Full record

ArticleInternational journal of biological macromolecules2020

S-adenosylmethionine synthases in plants: Structural characterization of type I and II isoenzymes from Arabidopsis thaliana and Medicago truncatula.

Bartosz Sekula, Milosz Ruszkowski, Zbigniew Dauter

Open access · greenAbstract read
In one paragraph

Article in International journal of biological macromolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

15 citing papers in PubMed, 58 citations in OpenAlex.

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  13. The Role of the mGenes · 2022
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  15. The dynamics of NGenome biology · 2021
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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

3 authors at 3 institutions in 2 countries.

Bartosz SekulaSynchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne, IL, USA. Electronic address: bartosz.sekula@nih.gov.
Milosz RuszkowskiSynchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne, IL, USA; Institute of Bioorganic Chemistry, Polish Academy of Sciences, Poznan, Poland.
Zbigniew DauterSynchrotron Radiation Research Section, Macromolecular Crystallography Laboratory, National Cancer Institute, Argonne, IL, USA.
Argonne National Laboratory · USInstitute of Bioorganic Chemistry, Polish Academy of Sciences · PLNational Cancer Institute · US

Funding

Macromolecular Crystallography Research with Synchrotron RadiationZIABC010378 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI DAUTER, ZBIGNIEW · 2009 to 2020
$18.8M
Time resolved SAXS studies on the RP2/Arl3 complex pp.484-485P41GM103622 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2012 to 2020
$11.9M
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
$529k
Intramural NIH HHS ZIA BC010378NIGMS NIH HHS P41 GM103622NIH HHS S10 OD018090
6 · The paper itself

Abstract

S-adenosylmethionine synthases (MATs) are responsible for production of S-adenosylmethionine, the cofactor essential for various methylation reactions, production of polyamines and phytohormone ethylene, etc. Plants have two distinct MAT types (I and II). This work presents the structural analysis of MATs from Arabidopsis thaliana (AtMAT1 and AtMAT2, both type I) and Medicago truncatula (MtMAT3a, type II), which, unlike most MATs from other domains of life, are dimers where three-domain subunits are sandwiched flat with one another. Although MAT types are very similar, their subunits are differently oriented within the dimer. Structural snapshots along the enzymatic reaction reveal the exact conformation of precatalytic methionine in the active site and show a binding niche, characteristic only for plant MATs, that may serve as a lock of the gate loop. Nevertheless, plants, in contrary to mammals, lack the MAT regulatory subunit, and the regulation of plant MAT activity is still puzzling. Our structures open a possibility of an allosteric activity regulation of type I plant MATs by linear compounds, like polyamines, which would tighten the relationship between S-adenosylmethionine and polyamine biosynthesis.

Indexed as

Models, MolecularProtein ConformationAmino Acid SequenceArabidopsisCatalytic DomainIsoenzymesLigandsMedicago truncatulaMethionine AdenosyltransferaseProtein BindingProtein MultimerizationS-AdenosylmethionineIsoenzymesLigandsMethionine AdenosyltransferaseS-AdenosylmethionineAdoMetMethionine adenosyltransferaseS-adenosylmethionine synthase

Identifiers

PMID32057875
PMCPMC8456715
OpenAlexW3005777848

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.