1pyg
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(New page: 200px<br /><applet load="1pyg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pyg, resolution 2.87Å" /> '''STRUCTURAL BASIS FOR...)
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Revision as of 22:06, 20 November 2007
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STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE
Overview
The three-dimensional structure of the activated state of glycogen, phosphorylase (GP) as induced by adenosine monophosphate (AMP) has been, determined from crystals of pyridoxalpyrophosphoryl-GP. The same, quaternary changes relative to the inactive conformation as those induced, by phosphorylation are induced by AMP, although the two regulatory signals, function through different local structural mechanisms. Moreover, previous, descriptions of the phosphorylase active state have been extended by, demonstrating that, on activation, the amino- and carboxyl-terminal, domains of GP rotate apart by 5 degrees, thereby increasing access of, substrates to the catalytic site. The structure also reveals previously, unobserved interactions with the nucleotide that accounts for the, specificity of the nucleotide binding site for AMP in preference to, inosine monophosphate.
About this Structure
1PYG is a Single protein structure of sequence from Oryctolagus cuniculus with AMP and PDP as ligands. Active as Phosphorylase, with EC number 2.4.1.1 Full crystallographic information is available from OCA.
Reference
Structural basis for the activation of glycogen phosphorylase b by adenosine monophosphate., Sprang SR, Withers SG, Goldsmith EJ, Fletterick RJ, Madsen NB, Science. 1991 Nov 29;254(5036):1367-71. PMID:1962195
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