Difference: TownleyShapiro07 (3 vs. 4)

Revision 428 Mar 2007 - Main.JasperShahn

 
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Townley, R, Shapiro, L. Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase. Science 315, 1726-9 ColumbiaUniversityintheCityofNewYorkcopy.gif
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Townley, R, Shapiro, L. Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase. Science 315: 1726-1729 ColumbiaUniversityintheCityofNewYorkcopy.gif
  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 levels. Here we report crystal structures at 2.6 and 2.9 Å resolution for ATP- and AMP-bound forms of a core αβγ adenylate-binding domain from the fission yeast AMPK homologue. ATP and AMP bind competitively to a single site in the γ subunit, with their respective phosphate groups positioned near function-impairing mutants. Surprisingly, ATP binds without counter ions, amplifying its electrostatic effects on a critical regulatory region where all three subunits converge.
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