Evidence map›Paper›PMID 23733187›Full record

ArticleThe Journal of biological chemistry2013

A novel family of soluble minimal scaffolds provides structural insight into the catalytic domains of integral membrane metallopeptidases.

Mar López-Pelegrín, Núria Cerdà-Costa, Francisco Martínez-Jiménez, Anna Cintas-Pedrola, Albert Canals, Juan R Peinado, Marc A Marti-Renom, Carlos López-Otín, Joan L Arolas, F Xavier Gomis-Rüth

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
–field-weighted citation impact
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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Proteomic Characterization of Antibiotic Resistance inInternational journal of molecular sciences · 2021
    Article
  9. Review
  10. OMA1-An integral membrane protease?Biochimica et biophysica acta. Proteins and proteomics · 2021
    Review
  11. Reversible autoinhibitory regulation ofProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  12. Article
  13. Article
  14. Article
  15. Constructing and deconstructing the bacterial cell wall.Protein science : a publication of the Protein Society · 2020
    Review
  16. Article
  17. Article
  18. Phosphoramidon inhibits the integral membrane protein zinc metalloprotease ZMPSTE24.Acta crystallographica. Section D, Structural biology · 2018
    Article
  19. Review
  20. 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

10 authors.

Mar López-PelegrínFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona.
Núria Cerdà-CostaFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona.
Francisco Martínez-Jiménezthe Genome Biology Group, Centre Nacional d'Anàlisi Genòmic, c/Baldiri Reixac, 4, 08028 Barcelona,; the Gene Regulation, Stem Cells and Cancer Program, Center for Genomic Regulation, c/Dr. Aiguader, 88, 08003 Barcelona.
Anna Cintas-PedrolaFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona.
Albert Canalsthe Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas and Institute for Research in Biomedicine, c/Baldiri Reixac, 10-12, 08028 Barcelona, and.
Juan R PeinadoFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona.
Marc A Marti-Renomthe Genome Biology Group, Centre Nacional d'Anàlisi Genòmic, c/Baldiri Reixac, 4, 08028 Barcelona,; the Gene Regulation, Stem Cells and Cancer Program, Center for Genomic Regulation, c/Dr. Aiguader, 88, 08003 Barcelona.
Carlos López-Otínthe Departamento de Bioquímica y Biología Molecular and Instituto Universitario de Oncología, Universidad de Oviedo, 33006 Oviedo, Spain.
Joan L ArolasFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona,. Electronic address: jlacri@ibmb.csic.es.
F Xavier Gomis-RüthFrom the Proteolysis Laboratory, Department of Structural Biology, Molecular Biology Institute of Barcelona, Consejo Superior de Investigaciones Científicas, c/Baldiri Reixac, 15-21, 08028 Barcelona,. Electronic address: xgrcri@ibmb.csic.es.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the search for structural models of integral-membrane metallopeptidases (MPs), we discovered three related proteins from thermophilic prokaryotes, which we grouped into a novel family called "minigluzincins." We determined the crystal structures of the zymogens of two of these (Pyrococcus abyssi proabylysin and Methanocaldococcus jannaschii projannalysin), which are soluble and, with ∼100 residues, constitute the shortest structurally characterized MPs to date. Despite relevant sequence and structural similarity, the structures revealed two unique mechanisms of latency maintenance through the C-terminal segments previously unseen in MPs as follows: intramolecular, through an extended tail, in proabylysin, and crosswise intermolecular, through a helix swap, in projannalysin. In addition, structural and sequence comparisons revealed large similarity with MPs of the gluzincin tribe such as thermolysin, leukotriene A4 hydrolase relatives, and cowrins. Noteworthy, gluzincins mostly contain a glutamate as third characteristic zinc ligand, whereas minigluzincins have a histidine. Sequence and structural similarity further allowed us to ascertain that minigluzincins are very similar to the catalytic domains of integral membrane MPs of the MEROPS database families M48 and M56, such as FACE1, HtpX, Oma1, and BlaR1/MecR1, which are provided with trans-membrane helices flanking or inserted into a minigluzincin-like catalytic domain. In a time where structural biochemistry of integral-membrane proteins in general still faces formidable challenges, the minigluzincin soluble minimal scaffold may contribute to our understanding of the working mechanisms of these membrane MPs and to the design of novel inhibitors through structure-aided rational drug design approaches.

Indexed as

Catalytic DomainAmino Acid SequenceArchaeaArchaeal ProteinsComputational BiologyCrystallography, X-RayEnzyme ActivationEnzyme AssaysEnzyme PrecursorsHumansMembrane ProteinsMetalloproteasesModels, MolecularMolecular Sequence DataProteolysisPyrococcusArchaeal ProteinsEnzyme PrecursorsMembrane ProteinsMetalloproteasesCatalytic DomainEnzyme MechanismsEnzyme StructureEnzymologyMembrane EnzymesMetallopeptidaseMetalloproteaseMolecular ModelMolecular ModelingZymogen

Identifiers

PMID23733187
PMCPMC3774397

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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.