Evidence map›Paper›PMID 24584934›Full record

ArticleThe Journal of biological chemistry2014

Structure and mechanism of soybean ATP sulfurylase and the committed step in plant sulfur assimilation.

Jonathan Herrmann, Geoffrey E Ravilious, Samuel E McKinney, Corey S Westfall, Soon Goo Lee, Patrycja Baraniecka, Marco Giovannetti, Stanislav Kopriva, Hari B Krishnan, Joseph M Jez

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. 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
2.1field-weighted citation impact, top 13% 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, 52 citations in OpenAlex.

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  9. Sulfation pathways from red to green.The Journal of biological chemistry · 2019
    Review
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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

10 authors at 4 institutions in 3 countries.

Jonathan HerrmannDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Geoffrey E RaviliousDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Samuel E McKinneyDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Corey S WestfallDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Soon Goo LeeDepartment of Biology, Washington University, St. Louis, Missouri 63130.
Patrycja BaranieckaJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Marco GiovannettiJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom; Department of Life Sciences and Systems Biology, University of Torino, Viale Mattioli 25, I-10125 Torino, Italy.
Stanislav KoprivaJohn Innes Centre, Norwich Research Park, Norwich NR4 7UH, United Kingdom.
Hari B KrishnanPlant Genetics Research Unit, United States Department of Agriculture-Agricultural Research Service, University of Missouri, Columbia, Missouri 65211.
Joseph M JezDepartment of Biology, Washington University, St. Louis, Missouri 63130. Electronic address: jjez@biology2.wustl.edu.
Washington University in St. Louis · USJohn Innes Centre · GBNorwich Research Park · GBUnited States Department of Agriculture · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Enzymes of the sulfur assimilation pathway are potential targets for improving nutrient content and environmental stress responses in plants. The committed step in this pathway is catalyzed by ATP sulfurylase, which synthesizes adenosine 5'-phosphosulfate (APS) from sulfate and ATP. To better understand the molecular basis of this energetically unfavorable reaction, the x-ray crystal structure of ATP sulfurylase isoform 1 from soybean (Glycine max ATP sulfurylase) in complex with APS was determined. This structure revealed several highly conserved substrate-binding motifs in the active site and a distinct dimerization interface compared with other ATP sulfurylases but was similar to mammalian 3'-phosphoadenosine 5'-phosphosulfate synthetase. Steady-state kinetic analysis of 20 G. max ATP sulfurylase point mutants suggests a reaction mechanism in which nucleophilic attack by sulfate on the α-phosphate of ATP involves transition state stabilization by Arg-248, Asn-249, His-255, and Arg-349. The structure and kinetic analysis suggest that ATP sulfurylase overcomes the energetic barrier of APS synthesis by distorting nucleotide structure and identifies critical residues for catalysis. Mutations that alter sulfate assimilation in Arabidopsis were mapped to the structure, which provides a molecular basis for understanding their effects on the sulfur assimilation pathway.

Indexed as

Adenosine PhosphosulfateAdenosine TriphosphateAmino Acid SequenceArabidopsisCatalysisCatalytic DomainCrystallography, X-RayGlycine maxHaplotypesHydrogen BondingKineticsMolecular Docking SimulationMolecular Sequence DataMutagenesis, Site-DirectedMutationProtein Structure, TertiaryAdenosine PhosphosulfateAdenosine TriphosphateSulfate AdenylyltransferaseSulfurEnzyme MechanismsEnzyme StructurePlantPlant BiochemistryProtein Structure

Identifiers

PMID24584934
PMCPMC4036203
OpenAlexW1977069279

What OpenQuestion holds

Textmetadata
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.