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- W2000233707 abstract "The 5'-AMP (adenosine monophosphate)-activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP (adenosine triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 and 2.6 A resolution for ATP- and AMP-bound forms of a core alphabetagamma adenylate-binding domain from the fission yeast AMPK homolog. ATP and AMP bind competitively to a single site in the gamma subunit, with their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, ATP binds without counterions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge." @default.
- W2000233707 created "2016-06-24" @default.
- W2000233707 creator A5060205129 @default.
- W2000233707 creator A5063445976 @default.
- W2000233707 date "2007-03-23" @default.
- W2000233707 modified "2023-09-23" @default.
- W2000233707 title "Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase" @default.
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- W2000233707 doi "https://doi.org/10.1126/science.1137503" @default.
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