1ygp: Difference between revisions
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'''PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.''' | {{Structure | ||
|PDB= 1ygp |SIZE=350|CAPTION= <scene name='initialview01'>1ygp</scene>, resolution 2.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=PLP:PYRIDOXAL-5'-PHOSPHATE'>PLP</scene> | |||
|ACTIVITY= | |||
|GENE= YEAST GLYCOGEN PHOSPHORYLASE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''PHOSPHORYLATED FORM OF YEAST GLYCOGEN PHOSPHORYLASE WITH PHOSPHATE BOUND IN THE ACTIVE SITE.''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1YGP is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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: yeast]] | [[Category: yeast]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:22:42 2008'' | ||
Revision as of 13:22, 20 March 2008
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| 1ygp, resolution 2.8Å | |||||||||||||
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| Ligands: | PO4 and PLP | ||||||||||||
| Gene: | YEAST GLYCOGEN PHOSPHORYLASE (Saccharomyces cerevisiae) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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. 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
Page seeded by OCA on Thu Mar 20 15:22:42 2008
