Comparison with previous crystal structures of active heterotrimers, with AMP at CBS3 and Thr172 phosphorylated, reveals a dramatic conformational change. This work reports the first structure, achieved using cryo-EM, of an inactive AMPK heterotrimer with an ATP analogue bound at CBS3 and Thr172 in a dephosphorylated state. Structure of an AMPK complex in an inactive, ATP-bound state. Deconvoluting AMP-activated protein kinase (AMPK) adenine nucleotide binding and sensing. AMPK structure and regulation from three angles. Structural basis for AMP binding to mammalian AMP-activated protein kinase. Structure of mammalian AMPK and its regulation by ADP. CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations. CBS domains: structure, function, and pathology in human proteins. Structural basis of AMPK regulation by adenine nucleotides and glycogen. Structural insight into the autoinhibition mechanism of AMP-activated protein kinase. Embryonic expression of AMPK gamma subunits and the identification of a novel γ2 transcript variant in adult heart. AMPK functions as an adenylate charge-regulated protein kinase. AMP-activated protein kinase: a cellular energy sensor that comes in 12 flavours. AMPK: sensing glucose as well as cellular energy status. AMPK: restoring metabolic homeostasis over space and time. AMPK and TOR: the Yin and Yang of cellular nutrient sensing and growth control. AMP-activated protein kinase: the current landscape for drug development.
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