Journal
PROTEIN SCIENCE
Volume 27, Issue 2, Pages 485-497Publisher
WILEY
DOI: 10.1002/pro.3340
Keywords
hydrogen-deuterium exchange; mass spectrometry; phosphorylase kinase; calmodulin; oligomeric proteins; molecular modeling
Categories
Funding
- National Institutes of Health [DK32953]
- KUMC Biomedical Research Training Program
- National Institute of Diabetes and Digestive and Kidney Diseases [DK32953]
- University of Kansas Medical Center [BRTP]
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In the tightly regulated glycogenolysis cascade, the breakdown of glycogen to glucose-1-phosphate, phosphorylase kinase (PhK) plays a key role in regulating the activity of glycogen phosphorylase. PhK is a 1.3 MDa hexadecamer, with four copies each of four different subunits (, , and ), making the study of its structure challenging. Using hydrogen-deuterium exchange, we have analyzed the regulatory subunit and the catalytic subunit in the context of the intact non-activated PhK complex to study the structure of these subunits and identify regions of surface exposure. Our data suggest that within the non-activated complex the subunit assumes an activated conformation and are consistent with a previous docking model of the subunit within the cryoelectron microscopy envelope of PhK.
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