2ooy

Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with ATP

spinqualitylabelsall models 2ooy, resolution 2.88Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ooy is a 6 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.88Å Ligands: ATP, FLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SNF1_SCHPO Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase.,Townley R, Shapiro L Science. 2007 Mar 23;315(5819):1726-9. Epub 2007 Feb 8. PMID:17289942 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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