Crystal Structures of the Adenylate Sensor from Fission Yeast AMP-Activated Protein Kinase
作者： R. Townley , L. Shapiro
关键词: Protein kinase A 、 Adenosine 、 Adenosine monophosphate 、 Adenylate kinase 、 Adenosine triphosphate 、 CBS domain 、 AMPK 、 Biochemistry 、 AMP-activated protein kinase 、 Biology 、 Biophysics
摘要: The 5′-AMP (adenosine monophosphate)–activated protein kinase (AMPK) coordinates metabolic function with energy availability by responding to changes in intracellular ATP triphosphate) and AMP concentrations. Here, we report crystal structures at 2.9 2.6 A resolution for ATP- AMP-bound forms of a core αβγ adenylate-binding domain from the fission yeast AMPK homolog. bind competitively single site γ subunit, their respective phosphate groups positioned near function-impairing mutants. Unexpectedly, binds without counterions, amplifying its electrostatic effects on critical regulatory region where all three subunits converge.
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