2oox

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(New page: 200px<br /><applet load="2oox" size="450" color="white" frame="true" align="right" spinBox="true" caption="2oox, resolution 2.60&Aring;" /> '''Crystal structure of...)
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Revision as of 11:07, 21 November 2007

Image:2oox.gif

2oox, resolution 2.60Å

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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 with AMP as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 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

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