Melcher, Karsten
Mayo Clinic
Department of Structural Biology, Van Andel Institute, Grand Rapids, MI 49503, USA. karsten.melcher@vai.org.
Citations 1
Structure of an AMPK complex in an inactive, ATP-bound state
Yan, Yan , Mukherjee, Somnath , Harikumar, Kaleeckal G. , Strutzenberg, Timothy S. , Zhou, X. Edward , Suino-Powell, Kelly, Xu, Ting-Hai , Sheldon, Ryan D. , Lamp, Jared , Brunzelle, J.S. , Radziwon, Katarzyna, Novick, Scott J. , Vega, Irving E. , Xu, H. Eric , Griffin, Patrick R. , Kossiakoff, Anthony A. , Melcher, Karsten , Brunzelle, Joseph S , Ellis, Abigail , Novick, Scott J , Jones, Russell G , Miller, Laurence J , Xu, H Eric , Griffin, Patrick R , Melcher, Karsten , Harikumar, Kaleeckal G , Jones, Russell G. , Miller, Laurence J.
Science | July 22, 2021 | Volume: 373 | Issue: 6553 | Pages: 413-419
How to catch a dynamic state AMP-activated protein kinase (AMPK) is a key sensor of energy status in eukaryotes. Its dynamic structure is regulated by allosteric factors including phosphorylation and binding of nucleotides and metabolites. Yan et al. developed conformation-specific antibodies that trap AMPK in a fully inactive state that has experienced a large, domain-level rotation. Biophysical experiments in cells and in vitro are consistent with the structural work and support a model in which the activation loop is fully exposed in the completely inactive, dephosphorylated state. These structures inform our understanding of the complex allosteric behavior in this crucial metabolic regulator. Science , abe7565, this issue p. 413