2oox
From Proteopedia
Crystal structure of the adenylate sensor from AMP-activated protein kinase complexed with AMP
Overview
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.
About this Structure
2OOX is a Protein complex structure of sequences from Schizosaccharomyces pombe. Full crystallographic information is available from OCA.
Reference
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 Page seeded by OCA on Sun May 4 11:21:19 2008
