1ygp

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

spinqualitylabelsall models 1ygp, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ygp is a 2 chain structure with sequence from Saccharomyces cerevisiae. The December 2001 RCSB PDB Molecule of the Month feature on Glycogen Phosphorylase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: PLP, PO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHSG_YEAST Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Glycogen Phosphorylase Glycogen phosphorylase 3D structures

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