Evidence map›Paper›PMID 19141288›Full record

ArticleStructure (London, England : 1993)2009

The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase.

Catherine Vénien-Bryan, Slavica Jonic, Vasiliki Skamnaki, Nick Brown, Nicolas Bischler, Nikos G Oikonomakos, Nicolas Boisset, Louise N Johnson

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

18 citing papers in PubMed, 35 citations in OpenAlex.

  1. Observational
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The regulation of glycogenolysis in the brain.The Journal of biological chemistry · 2018
    Review
  10. Review
  11. Article
  12. Protein post-translational modifications:Computational and structural biotechnology journal · 2017
    Review
  13. Article
  14. Article
  15. Article
  16. Louise N. Johnson 1940-2012.Nature structural & molecular biology · 2012
    Article
  17. Article
  18. 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

8 authors at 3 institutions in 3 countries.

Catherine Vénien-BryanLaboratory of Molecular Biophysics, Department of Biochemistry, University of Oxford, South Parks Road, OX1 3QU Oxford, UK. catherine.venien@bioch.ox.ac.uk
Slavica Jonic
Vasiliki Skamnaki
Nick Brown
Nicolas Bischler
Nikos G Oikonomakos
Nicolas Boisset
Louise N Johnson
MRC Laboratory of Molecular Biology · GBNational Hellenic Research Foundation · GRInstitut de minéralogie, de physique des matériaux et de cosmochimie · FR

Funding

Wellcome Trust 064775
6 · The paper itself

Abstract

Phosphorylase kinase (PhK) coordinates hormonal and neuronal signals to initiate the breakdown of glycogen. The enzyme catalyzes the phosphorylation of inactive glycogen phosphorylase b (GPb), resulting in the formation of active glycogen phosphorylase a. We present a 9.9 angstroms resolution structure of PhK heterotetramer (alphabetagammadelta)4 determined by cryo-electron microscopy single-particle reconstruction. The enzyme has a butterfly-like shape comprising two lobes with 222 symmetry. This three-dimensional structure has allowed us to dock the catalytic gamma subunit to the PhK holoenzyme at a location that is toward the ends of the lobes. We have also determined the structure of PhK decorated with GPb at 18 angstroms resolution, which shows the location of the substrate near the kinase subunit. The PhK preparation contained a number of smaller particles whose structure at 9.8 angstroms resolution was consistent with a proteolysed activated form of PhK that had lost the alpha subunits and possibly the gamma subunits.

Indexed as

Catalytic DomainChromatography, GelCryoelectron MicroscopyCrystallography, X-RayElectrophoresis, Polyacrylamide GelGlycogen PhosphorylaseModels, MolecularPhosphorylase KinaseProtein ConformationSubstrate SpecificityGlycogen PhosphorylasePhosphorylase Kinase

Identifiers

PMID19141288
PMCPMC2639635
OpenAlexW1978058960

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.