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1ygp

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[[Image:1ygp.jpg|left|200px]]
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[[Image:1ygp.png|left|200px]]
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==Overview==
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{{ABSTRACT_8703213}}
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A phosphorylation-initiated mechanism of local protein refolding activates yeast glycogen phosphorylase (GP). Refolding of the phosphorylated amino-terminus was shown to create a hydrophobic cluster that wedges into the subunit interface of the enzyme to trigger activation. The phosphorylated threonine is buried in the allosteric site. The mechanism implicates glucose 6-phosphate, the allosteric inhibitor, in facilitating dephosphorylation by dislodging the buried covalent phosphate through binding competition. Thus, protein phosphorylation-dephosphorylation may also be controlled through regulation of the accessibility of the phosphorylation site to kinases and phosphatases. In mammalian glycogen phosphorylase, phosphorylation occurs at a distinct locus. The corresponding allosteric site binds a ligand activator, adenosine monophosphate, which triggers activation by a mechanism analogous to that of phosphorylation in the yeast enzyme.
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==About this Structure==
==About this Structure==
1YGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1YGP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb24_1.html Glycogen Phosphorylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGP OCA].
1YGP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. The following page contains interesting information on the relation of 1YGP with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb24_1.html Glycogen Phosphorylase]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YGP OCA].
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==Reference==
 
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A protein phosphorylation switch at the conserved allosteric site in GP., Lin K, Rath VL, Dai SC, Fletterick RJ, Hwang PK, Science. 1996 Sep 13;273(5281):1539-42. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8703213 8703213]
 
[[Category: Glycogen Phosphorylase]]
[[Category: Glycogen Phosphorylase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Phosphorylated form]]
[[Category: Phosphorylated form]]
[[Category: Yeast]]
[[Category: Yeast]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:17:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 26 18:08:05 2008''

Revision as of 15:08, 26 June 2008

Image:1ygp.png

Template:STRUCTURE 1ygp

PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.


Template:ABSTRACT 8703213

About this Structure

1YGP is a Single protein structure of sequence from Saccharomyces cerevisiae. The following page contains interesting information on the relation of 1YGP with [Glycogen Phosphorylase]. Full crystallographic information is available from OCA.

Page seeded by OCA on Thu Jun 26 18:08:05 2008

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