Evidence map›Paper›PMID 22961982›Full record

ArticleThe Journal of biological chemistry2012

Crystal structure of Arabidopsis Deg2 protein reveals an internal PDZ ligand locking the hexameric resting state.

Renhua Sun, Haitian Fan, Feng Gao, Yajing Lin, Lixin Zhang, Weimin Gong, Lin Liu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. 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
1.3field-weighted citation impact, top 20% 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, 35 citations in OpenAlex.

  1. NAL1 forms a molecular cage to regulate FZP phase separation.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The structures of Arabidopsis Deg5 and Deg8 reveal new insights into HtrA proteases.Acta crystallographica. Section D, Biological crystallography · 2013
    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

7 authors at 4 institutions in 3 countries.

Renhua SunPhotosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
Haitian Fan
Feng Gao
Yajing Lin
Lixin Zhang
Weimin Gong
Lin Liu
Chinese Academy of Sciences · CNCzech Academy of Sciences, Institute of Biophysics · CZInstitute of Botany · CNInstitute of Botany of the Slovak Academy of Sciences · SK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Eukaryotic organelles have developed elaborate protein quality control systems to ensure their normal activity, among which Deg/HtrA proteases play an essential role. Plant Deg2 protease is a homologue of prokaryotic DegQ/DegP proteases and is located in the chloroplast stroma, where its proteolytic activity is required to maintain the efficiency of photosynthetic machinery during stress. Here, we demonstrate that Deg2 exhibits dual protease-chaperone activities, and we present the hexameric structure of Deg2 complexed with co-purified peptides. The structure shows that Deg2 contains a unique second PDZ domain (PDZ2) following a conventional PDZ domain (PDZ1), with PDZ2 orchestrating the cage assembly of Deg2. We discovered a conserved internal ligand for PDZ2 that mediates hexamer formation and thus locks the protease in the resting state. These findings provide insight into the diverse modes of PDZ domain-mediated regulation of Deg proteases.

Indexed as

ArabidopsisArabidopsis ProteinsCaseinsCrystallography, X-RayHydrogen BondingHydrogen-Ion ConcentrationLigandsProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProteolysisSerine EndopeptidasesArabidopsis ProteinsCaseinsDeg2 protein, ArabidopsisLigandsSerine Endopeptidases

Identifiers

PMID22961982
PMCPMC3481350
OpenAlexW2169306264

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.