Crystallization of the glycogen‐binding domain of the AMP‐activated protein kinase β subunit and preliminary X‐ray analysis

AMP‐activated protein kinase (AMPK) is an intracellular energy sensor that regulates metabolism in response to energy demand and supply by adjusting the ATP‐generating and ATP‐consuming pathways. AMPK potentially plays a critical role in diabetes and obesity as it is known to be activated by metforin and rosiglitazone, drugs used for the treatment of type II diabetes. AMPK is a heterotrimer composed of a catalytic α subunit and two regulatory subunits, β and γ. Mutations in the γ subunit are known to cause glycogen accumulation, leading to cardiac arrhythmias. Recently, a functional glycogen‐binding domain (GBD) has been identified in the β subunit. Here, the crystallization of GBD in the presence of β‐cyclodextrin is reported together with preliminary X‐ray data analysis allowing the determination of the structure by single isomorphous replacement and threefold averaging using in‐house X‐ray data collected from a selenomethionine‐substituted protein.