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| Title | The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase. |
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| Journal, issue, pages | Structure, Vol. 17, Issue 1, Page 117-127, Year 2009 |
| Publish date | Jan 14, 2009 |
 Authors | Catherine Vénien-Bryan / Slavica Jonic / Vasiliki Skamnaki / Nick Brown / Nicolas Bischler / Nikos G Oikonomakos / Nicolas Boisset / Louise N Johnson /  |
| PubMed 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), ...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. |
 External links | Structure / PubMed:19141288 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 9.9 Å |
| Structure data |  EMDB-1527: |
| Source |
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Oryctolagus cuniculus (rabbit)