1ygp
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(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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Revision as of 07:00, 18 November 2007
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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 PO4 and PLP 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
Page seeded by OCA on Sun Nov 18 09:07:16 2007
