The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase.
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....
Vénien-Bryan, C., Jonic, S., Skamnaki, V., Brown, N., Bischler, N., Oikonomakos, N. G., Boisset, N., & Johnson, L. N. (2009). The structure of phosphorylase kinase holoenzyme at 9.9 angstroms resolution and location of the catalytic subunit and the substrate glycogen phosphorylase. Structure (London, England : 1993), 17(1), 117–127.
Vénien-Bryan, C., et al. "The Structure of Phosphorylase Kinase Holoenzyme at 9.9 Angstroms Resolution and Location of the Catalytic Subunit and the Substrate Glycogen Phosphorylase." Structure (London, England : 1993), vol. 17, no. 1, 2009, pp. 117–27.
Vénien-Bryan, C, S Jonic, V Skamnaki, N Brown, N Bischler, NG Oikonomakos, N Boisset, and LN Johnson. 2009. "The Structure of Phosphorylase Kinase Holoenzyme at 9.9 Angstroms Resolution and Location of the Catalytic Subunit and the Substrate Glycogen Phosphorylase." Structure (London, England : 1993) 17 (1): 117–27.
10.1016/j.str.2008.10.013
+ Vénien-Bryan, C More by this author
+ Jonic, S More by this author
+ Skamnaki, V More by this author
+ Brown, N More by this author
+ Bischler, N More by this author
Structure (London, England : 1993)
uuid:fc5e2b47-fd29-4e14-b2ff-9fa4ad5f6fe7
Chromatography, Gel
Models, Molecular
Substrate Specificity
Electrophoresis, Polyacrylamide Gel
Phosphorylase Kinase
Catalytic Domain
Cryoelectron Microscopy