Fig. 1: Overall structure of the PhK holoenzyme.
From: Architecture and activation of human muscle phosphorylase kinase
a Size-exclusion chromatography of the inactive PhK holoenzyme. b SDS–PAGE analysis of the inactive PhK holoenzyme. This experiment has been repeated at least three times. c Recombinant PhK displays Ca2+-dependent kinase activity. The phosphorylation of human muscle phosphorylase (PYGM) was examined by immunoblotting using a phospho-specific antibody. This experiment has been repeated at least three times. d The structural model of the PhK hexadecamer is shown in two orientations. The β-subunits are shown in different shades of green; whereas the α-, γ-, and δ-subunits are shown in gold, cyan, and dark blue, respectively. e Local cryo-EM density map of the αβγδ heterotetramer shown in two orientations, with the structural model enclosed.
