1ygp
From Proteopedia
(New page: 200px<br /> <applet load="1ygp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ygp, resolution 2.8Å" /> '''PHOSPHORYLATED FORM ...) |
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caption="1ygp, resolution 2.8Å" /> | caption="1ygp, resolution 2.8Å" /> | ||
'''PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.'''<br /> | '''PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with PO4 and PLP as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 1YGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=PLP:'>PLP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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]. |
==Reference== | ==Reference== | ||
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[[Category: yeast]] | [[Category: yeast]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 17:12:05 2008'' |
Revision as of 15:12, 15 February 2008
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PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.
Overview
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.
About this Structure
1YGP is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. The following page contains interesting information on the relation of 1YGP with [Glycogen Phosphorylase]. Full crystallographic information is available from OCA.
Reference
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:8703213
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