Evidence map›Paper›PMID 19805099›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Structural basis for Ca2+-independence and activation by homodimerization of tomato subtilase 3.

Christian Ottmann, Rolf Rose, Franziska Huttenlocher, Anna Cedzich, Patrick Hauske, Markus Kaiser, Robert Huber, Andreas Schaller

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

49 citing papers in PubMed, 89 citations in OpenAlex.

  1. Natural Variation of NAR5 Determines Nitrogenase Activity and the Yield in Soybean.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  3. Journal of agricultural and food chemistry · 2026
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  16. Processing of a plant peptide hormone precursor facilitated by posttranslational tyrosine sulfation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. HYL1-CLEAVAGE SUBTILASE 1 (HCS1) suppresses miRNA biogenesis in response to light-to-dark transition.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  18. Article
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  20. Structure, dynamics and immunogenicity of a catalytically inactive CComputational and structural biotechnology journal · 2020
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 1 country.

Christian OttmannChemical Genomics Centre, Otto-Hahn-Strasse 15, 44227 Dortmund, Germany.
Rolf Rose
Franziska Huttenlocher
Anna Cedzich
Patrick Hauske
Markus Kaiser
Robert Huber
Andreas Schaller
University of Hohenheim · DEMax Planck Institute of Molecular Physiology · DEMax Planck Society · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Subtilases are serine proteases found in Archae, Bacteria, yeasts, and higher eukaryotes. Plants possess many more of these subtilisin-like endopeptidases than animals, e.g., 56 identified genes in Arabidopsis compared with only 9 in humans, indicating important roles for subtilases in plant biology. We report the first structure of a plant subtilase, SBT3 from tomato, in the active apo form and complexed with a chloromethylketone (cmk) inhibitor. The domain architecture comprises an N-terminal protease domain displaying a 132 aa protease-associated (PA) domain insertion and a C-terminal seven-stranded jelly-roll fibronectin (Fn) III-like domain. We present the first structural evidence for an explicit function of PA domains in proteases revealing a vital role in the homo-dimerization of SBT3 and in enzyme activation. Although Ca(2+)-binding sites are conserved and critical for stability in other subtilases, SBT3 was found to be Ca(2+)-free and its thermo stability is Ca(2+)-independent.

Indexed as

Protein Structure, TertiaryCalciumCatalytic DomainCrystallizationEnzyme ActivationEnzyme StabilityModels, MolecularMutagenesis, Site-DirectedProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondarySolanum lycopersicumSubtilisinsCalciumsubtilase, plantSubtilisins

Identifiers

PMID19805099
PMCPMC2749846
OpenAlexW2140256954

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.