1pyg: Difference between revisions

Revision as of 15:33, 21 February 2008

STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE

OverviewOverview

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 StructureAbout this Structure

1PYG is a Single protein structure of sequence from Oryctolagus cuniculus with and as ligands. Active as Phosphorylase, with EC number 2.4.1.1 Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 14:33:54 2008

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OCA

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-[[Image:1pyg.jpg|left|200px]]<br /><applet load="1pyg" size="450" color="white" frame="true" align="right" spinBox="true"
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 caption="1pyg, resolution 2.87&Aring;" />
 '''STRUCTURAL BASIS FOR THE ACTIVATION OF GLYCOGEN PHOSPHORYLASE B BY ADENOSINE MONOPHOSPHATE'''<br />
 ==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.
+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==
-PYG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with AMP and PDP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PYG OCA].
+PYG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=PDP:'>PDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PYG OCA].
 ==Reference==
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 [[Category: glycogen phosphorylase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:14:01 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:33:54 2008''